Category: 7. Science

  • New Fossils Reveal Humans’ Mysterious Lost Cousin

    New Fossils Reveal Humans’ Mysterious Lost Cousin

    Newly discovered teeth from Ethiopia reveal that early humans coexisted with a mysterious cousin species, reshaping our understanding of human origins. Credit: Shutterstock

    Fossils uncovered in northeastern Ethiopia, dating to between 2.6 and 2.8 million years ago, provide new insights into the course of human evolution.

    An international team of researchers has uncovered new fossils in Africa showing that Australopithecus and the earliest known members of Homo lived in the same region at the same time, between 2.6 and 2.8 million years ago. Among the finds was a previously unknown species of Australopithecus, unlike any identified before.

    The discoveries come from the Ledi-Geraru Research Project, led by scientists at Arizona State University. This site has already produced the world’s oldest known Homo specimen, as well as the earliest examples of Oldowan stone tools.

    Fossil Teeth From Ledi Geraru Research Area
    The 13 fossil teeth collected in the Ledi-Geraru Research Area from 2015 to 2018. The collections at LD 750 and LD 760 localities represent a newly discovered species of Australopithecus. LD 302 and AS 100 represent early Homo already known from the LD 350 mandible discovered in 2013. Credit: Brian Villmoare/University of Nevada, Las Vegas

    Detailed study of the newly recovered Australopithecus teeth confirmed that they represent a distinct species rather than belonging to Australopithecus afarensis, the species of the famous fossil “Lucy.” This finding reinforces that no remains of Lucy’s lineage are known to be younger than 2.95 million years.

    “This new research shows that the image many of us have in our minds of an ape to a Neanderthal to a modern human is not correct — evolution doesn’t work like that,” said ASU paleoecologist Kaye Reed. “Here we have two hominin species that are together. And human evolution is not linear, it’s a bushy tree, there are life forms that go extinct.”

    Examining Turtle Flat Teeth
    “These are teeth from Turtle Flat as we were discovering them — you can see what the ground behind looked like, and how amazing it was that Omar Abdulla first saw them on the surface,” said Amy Rector, Virginia Commonwealth University scientist. Credit: Amy Rector, Virginia Commonwealth University

    A research effort spanning decades

    Reed serves as a Research Scientist at the Institute of Human Origins and is a President’s Professor Emerita in the School of Human Evolution and Social Change at Arizona State University. She has also co-directed the Ledi-Geraru Research Project since 2002.

    So what fossils helped shape these new conclusions? The team uncovered 13 teeth in total.

    The Ledi-Geraru site has drawn attention before. In 2013, Reed and her colleagues reported the discovery of the earliest known Homo fossil—a jaw dating to 2.8 million years ago. The new study builds on that legacy, describing additional teeth from the site that belong to both the genus Homo and a newly identified species of Australopithecus.

    Lucas Delezene Compares One of the Incisors
    University of Arkansas Associate Professor Lucas Delezene compares one of the incisors the team discovered to an Australopithecus maxilla (upper jaw) from Hadar at the National Museum of Ethiopia. Credit: Amy Rector

    “The new finds of Homo teeth from 2.6 – 2.8 million-year-old sediments, reported in this paper, confirm the antiquity of our lineage,” said Brian Villmoare, lead author and ASU alumnus.

    “We know what the teeth and mandible of the earliest Homo look like, but that’s it. This emphasizes the critical importance of finding additional fossils to understand the differences between Australopithecus and Homo, and potentially how they were able to overlap in the fossil record at the same location.”

    The team cannot name the species yet based on the teeth alone; more fossils are needed before that can happen.

    How do scientists know these fossil teeth are millions of years old?

    Volcanoes.

    The Afar region remains an active rift zone, marked by frequent volcanic and tectonic activity. When these volcanoes erupted, they released ash containing crystals known as feldspars, which provide scientists with a way to determine their age, explained Christopher Campisano, a geologist at ASU.

    Lee Adoyta Basin
    Ledi-Geraru paleontological team searching for fossils in the Lee Adoyta Basin, where the genera Homo and Australopithecus have been recovered. Credit: Kaye Reed, Arizona State University

    “We can date the eruptions that were happening on the landscape when they’re deposited,” said Campisano, a Research Scientist at the Institute of Human Origins and Associate Professor at the School of Human Evolution and Social Change.

    “And we know that these fossils are interbed between those eruptions, so we can date units above and below the fossils. We are dating the volcanic ash of the eruptions that were happening while they were on the landscape.”

    Location of the Ledi Geraru Site and Australopithecus
    Maps showing (left) the location of the Ledi‑Geraru site within the Horn of Africa, and (right) the location of the Australopithecus and Homo teeth. Credit: Erin DiMaggio

    Ledi-Geraru’s ancient landscape

    Finding fossils and dating the landscape not only helps scientists understand the species, but it also helps them recreate the environment millions of years ago. The modern faulted badlands of Ledi-Geraru, where the fossils were found, are a stark contrast to the landscape these hominins traversed 2.6 – 2.8 million years ago. Back then, rivers migrated across a vegetated landscape into shallow lakes that expanded and contracted over time.

    Ramon Arrowsmith, a geologist at ASU, has been working with the Ledi-Geraru Research Project since 2002. He explained the area has an interpretable geologic record with good age control for the geologic time range of 2.3 to 2.95 million years ago.

    L to R Ramon Arrowsmith, Emeritus Kaye Reed and Christopher Campisano
    From left: Arizona State University Professor Ramon Arrowsmith, President’s Professor Emeritus Kaye Reed and Associate Professor Christopher Campisano discussing the Homo teeth that were found in the Asboli, an area at the Ledi‑Geraru site. Credit: Eric Scott

    “It is a critical time period for human evolution as this new paper shows,” said Arrowsmith, professor at the School of Earth and Space Exploration. “The geology gives us the age and characteristics of the sedimentary deposits containing the fossils. It is essential for age control.”

    Reed said the team is examining tooth enamel now to find out what they can about what these species were eating. There are still remaining questions the team will continue to work on.

    Were the early Homo and this unidentified species of Australopithecus eating the same things? Were they fighting for or sharing resources? Did they pass each other daily? Who were the ancestors of these species?

    No one knows – yet.

    Ledi Geraru Research Team
    Ledi‑Geraru research team, 2025. Credit: Amy Rector

    “Whenever you have an exciting discovery, if you’re a paleontologist, you always know that you need more information,” said Reed. “You need more fossils. That’s why it’s an important field to train people in and for people to go out and find their own sites and find places that we haven’t found fossils yet.”

    “More fossils will help us tell the story of what happened to our ancestors a long time ago — but because we’re the survivors, we know that it happened to us.”

    Reference: “New discoveries of Australopithecus and Homo from Ledi-Geraru, Ethiopia” by Brian Villmoare, Lucas K. Delezene, Amy L. Rector, Erin N. DiMaggio, Christopher J. Campisano, David A. Feary, Baro’o Mohammed Ali, Daniel Chupik, Alan L. Deino, Dominique I. Garello, Mohammed Ahmeddin Hayidara, Ellis M. Locke, Omar Abdulla Omar, Joshua R. Robinson, Eric Scott, Irene E. Smail, Kebede Geleta Terefe, Lars Werdelin, William H. Kimbel, J. Ramón Arrowsmith and Kaye E. Reed, 13 August 2025, Nature.
    DOI: 10.1038/s41586-025-09390-4

    Funding: U.S. National Science Foundation

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  • Ancient oxygen surge reshaped ocean life

    Ancient oxygen surge reshaped ocean life

    Roughly 390 million years ago, the ancient seas witnessed a dramatic change. Marine animals began moving into deeper waters that had long been uninhabitable. New research suggests this expansion was fueled by a lasting rise in deep-ocean oxygen.

    The source of that oxygen traces back to the spread of woody plants on land, the earliest forests on Earth. This environmental shift coincided with an explosion of new species, especially jawed fish.


    These fish became the ancestors of nearly all vertebrates alive today. The link between oxygen levels and evolutionary diversification offers fresh insight into how life reshaped the oceans.

    Oxygen rise shaped evolution

    “It’s known that oxygen is a necessary condition for animal evolution, but the extent to which it is the sufficient condition that can explain trends in animal diversification has been difficult to pin down,” said co-lead author Michael Kipp, assistant professor at Duke University.

    “This study gives a strong vote that oxygen dictated the timing of early animal evolution, at least for the appearance of jawed vertebrates in deep-ocean habitats.”

    For decades, scientists believed deep-ocean oxygenation occurred only once, at the start of the Paleozoic Era about 540 million years ago.

    Later evidence pointed instead to multiple phases. First, shallower waters became livable for breathing organisms, and only later did oxygen reach deeper environments.

    Rocks reveal ocean oxygen history

    Kipp and his colleagues focused on timing by studying sedimentary rocks once buried beneath ancient oceans.

    They measured levels of selenium, an element that records traces of oxygen in the environment. Selenium occurs in different isotopes, and their ratios reveal whether oxygen levels were high enough to support animal life.

    The team collected 97 rock samples dating from 252 to 541 million years ago, gathered from five continents.

    At the time, these sites lay along outer continental shelves, the zones where land tapered into the ocean before plunging steeply downward. By analyzing isotope ratios in the samples, the researchers tracked oxygen’s reach through time.

    Two deep-sea oxygen waves

    Results showed two distinct deep-ocean oxygenation events. One brief episode occurred during the Cambrian period, about 540 million years ago.

    The second began during the Middle Devonian, around 393 to 382 million years ago, and continues today. Between these events, oxygen dropped to inhospitable levels for most animals.

    “The selenium data tell us that the second oxygenation event was permanent. It began in the Middle Devonian and persisted in our younger rock samples,” said co-lead author Kunmanee “Mac” Bubphamanee, a Ph.D. candidate at the University of Washington.

    Vertebrates thrived with more oxygen

    The Middle Devonian oxygen rise triggered what scientists call the “mid-Paleozoic marine revolution.” With oxygen now plentiful, jawed fish and other animals expanded into deeper waters and diversified.

    Fossil evidence also shows that many species grew larger, likely supported by the richer oxygen supply. One example is shown in the featured image of this article – a prehistoric jawed fish from the Late Devonian called Dunkleosteus.

    This geological shift aligned with another event on land: the spread of woody plants.

    “Our thinking is that, as these woody plants increased in number, they released more oxygen into the air, which led to more oxygen in deeper ocean environments,” Kipp said.

    First oxygen wave faded fast

    The earlier Cambrian oxygen surge remains puzzling. Its decline likely prevented animals from permanently establishing themselves in deeper waters at that time.

    “What seems clear is that the drop in oxygen after that initial pulse hindered the spread and diversification of marine animals into those deeper environments of the outer continental shelves,” Kipp noted.

    Oxygen history warns about today’s oceans

    Although the study looks far into the past, its message carries urgency now.

    “Today, there’s abundant ocean oxygen in equilibrium with the atmosphere,” said Kipp. “But in some locations, ocean oxygen can drop to undetectable levels.”

    “Some of these zones occur through natural processes. But in many cases, they’re driven by nutrients draining off continents from fertilizers and industrial activity that fuel plankton blooms that suck up oxygen when they decay.”

    “This work shows very clearly the link between oxygen and animal life in the ocean. This was a balance struck about 400 million years ago, and it would be a shame to disrupt it today in a matter of decades.”

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    Featured image: An artist’s rendering of a prehistoric jawed fish from the Late Devonian called Dunkleosteus. These sorts of large, active vertebrates evolved shortly after the deep ocean became well-oxygenated. Credit: 2008 N. Tamura/CC-BY-SA

    The study is published in the journal Proceedings of the National Academy of Sciences.

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  • How Did Cavefish Lose Their Eyes?

    How Did Cavefish Lose Their Eyes?

    Small, colorless, and blind, amblyopsid cavefishes inhabit subterranean waters throughout the eastern United States. In a new study, Yale researchers reveal insights into just how these distinctive cave dwellers evolved — and provide a unique method for dating the underground ecosystems where they reside.

    In an analysis of the genomes of all known amblyopsid species, the researchers found that the different species colonized caves systems independently of each other and separately evolved similar traits — such as the loss of eyes and pigment — as they adapted to their dark cave environments.

    Their findings are published in the journal Molecular Biology and Evolution.

    By studying the genetic mutations that caused the fishes’ eyes to degenerate, the researchers developed a sort of mutational clock that allowed them to estimate when each species began losing their eyes. They found that vision-related genes of the oldest cavefish species, the Ozark cavefish (Troglichthys rosae), began degenerating up to 11 million years ago. 

    The technique provides a minimum age for the caves that the fishes colonized since the cavefish must have been inhabiting subterranean waters when their eyesight began devolving, the researchers said.

    “The ancient subterranean ecosystems of eastern North America are very challenging to date using traditional geochronological cave-dating techniques, which are unreliable beyond an upper limit of about 3 to 5 million years,” said Chase Brownstein, a student in Yale’s Graduate School of Arts and Sciences, in the Department of Ecology & Evolutionary Biology, and the study’s co-lead author. “Determining the ages of cave-adapted fish lineages allows us to infer the minimum age of the caves they inhabit because the fishes wouldn’t have started losing their eyes while living in broad daylight. In this case we estimate a minimum age of some caves of over 11 million years.”

    Maxime Policarpo of the Max Planck Institute for Biological Intelligence and the University of Basel is the co-lead author.

    For the study, the researchers reconstructed a time-calibrated evolutionary tree for amblyopsids, which belong to an ancient, species-poor order of freshwater fishes called Percopsiformes, using the fossil record as well as genomic data and high-resolution scans of all living relevant species. 

    All the cavefish species have similar anatomies, including elongated bodies and flattened skulls, and their pelvic fins have either been lost or severely reduced. Swampfish (Chologaster cornuta), a sister to cavefish lineage that inhabits murky surface waters, also has a flattened skull, elongated body, and no pelvic fin. While it maintains sight and pigment, there is softening of the bones around its eyes, which disappear in cavefishes. This suggests that cavefishes evolved from a common ancestor that was already equipped to inhabit low-light environments, Brownstein said. 

    To understand when the cavefish began populating caves — something impossible to discern from the branches of an evolutionary tree — the researchers studied the fishes’ genomes, examining 88 vision-related genes for mutations. The analysis revealed that the various cavefish lineages had completely different sets of genetic mutations involved in the loss of vision. This, they said, suggests that separate species colonized caves and adapted to those subterranean ecosystems independently of each other. 

    From there, the researchers developed a method for calculating the number of generations that have passed since cavefish species began adapting to life in caves by losing the functional copies of vision-related genes. 

    Their analysis suggests that cave adaptations occurred between 2.25 and 11.3 million years ago in Ozark cavefish and between 342,000 to 1.70 million years ago (at minimum) and 1.7 to 8.7 million years ago (at maximum) for other cavefish lineages. The findings support the conclusion that at least four amblyopsid lineages independently colonized caves after evolving from surface-dwelling ancestors, the researchers said. 

    The maximum ages exceed the ranges of traditional cave-dating methods, which includes isotope analysis of cosmogenic nuclides that are produced within rocks and soils by cosmic rays, the researchers noted.

    The findings also suggest potential implications for human health, said Thomas Near, professor of ecology and evolutionary biology in Yale’s Faculty of Arts and Sciences (FAS), and senior author of the study. 

    “A number of the mutations we see in the cavefish genomes that lead to degeneration of the eyes are similar to mutations that cause ocular diseases in humans,” said Near, who is also the Bingham Oceanographic Curator of Ichthyology at the Yale Peabody Museum. “There is the possibility for translational medicine through which by studying this natural system in cavefishes, we can glean insights into the genomic mechanisms of eye diseases in humans.”

    Reference: Brownstein CD, Policarpo M, Harrington RC, et al. Convergent evolution in amblyopsid cavefishes and the age of eastern north american subterranean ecosystems. Mol Biol Evol. 2025;42(8):msaf185. doi: 10.1093/molbev/msaf185

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  • Localized Translation at Mitochondria Decoded by Scientists

    Localized Translation at Mitochondria Decoded by Scientists

    Our cells produce a variety of proteins, each with a specific role that, in many cases, means that they need to be in a particular part of the cell where that role is needed. One of the ways that cells ensure certain proteins end up in the right location at the right time is through localized translation, a process that ensures that proteins are made — or translated — close to where they will be needed. MIT professor of biology and Whitehead Institute for Biomedical Research member Jonathan Weissman and colleagues have studied localized translation in order to understand how it affects cell functions and allows cells to quickly respond to changing conditions.

    Now, Weissman, who is also a Howard Hughes Medical Institute Investigator, and postdoc in his lab Jingchuan Luo have expanded our knowledge of localized translation at mitochondria, structures that generate energy for the cell. In an open-access paper published today in Cell, they share a new tool, LOCL-TL, for studying localized translation in close detail, and describe the discoveries it enabled about two classes of proteins that are locally translated at mitochondria.

    The importance of localized translation at mitochondria relates to their unusual origin. Mitochondria were once bacteria that lived within our ancestors’ cells. Over time, the bacteria lost their autonomy and became part of the larger cells, which included migrating most of their genes into the larger cell’s genome in the nucleus. Cells evolved processes to ensure that proteins needed by mitochondria that are encoded in genes in the larger cell’s genome get transported to the mitochondria. Mitochondria retain a few genes in their own genome, so production of proteins from the mitochondrial genome and that of the larger cell’s genome must be coordinated to avoid mismatched production of mitochondrial parts. Localized translation may help cells to manage the interplay between mitochondrial and nuclear protein production — among other purposes.

    How to detect local protein production

    For a protein to be made, genetic code stored in DNA is read into RNA, and then the RNA is read or translated by a ribosome, a cellular machine that builds a protein according to the RNA code. Weissman’s lab previously developed a method to study localized translation by tagging ribosomes near a structure of interest, and then capturing the tagged ribosomes in action and observing the proteins they are making. This approach, called proximity-specific ribosome profiling, allows researchers to see what proteins are being made where in the cell. The challenge that Luo faced was how to tweak this method to capture only ribosomes at work near mitochondria.

    Ribosomes work quickly, so a ribosome that gets tagged while making a protein at the mitochondria can move on to making other proteins elsewhere in the cell in a matter of minutes. The only way researchers can guarantee that the ribosomes they capture are still working on proteins made near the mitochondria is if the experiment happens very quickly.

    Weissman and colleagues had previously solved this time sensitivity problem in yeast cells with a ribosome-tagging tool called BirA that is activated by the presence of the molecule biotin. BirA is fused to the cellular structure of interest, and tags ribosomes it can touch — but only once activated. Researchers keep the cell depleted of biotin until they are ready to capture the ribosomes, to limit the time when tagging occurs. However, this approach does not work with mitochondria in mammalian cells because they need biotin to function normally, so it cannot be depleted.

    Luo and Weissman adapted the existing tool to respond to blue light instead of biotin. The new tool, LOV-BirA, is fused to the mitochondrion’s outer membrane. Cells are kept in the dark until the researchers are ready. Then they expose the cells to blue light, activating LOV-BirA to tag ribosomes. They give it a few minutes and then quickly extract the ribosomes. This approach proved very accurate at capturing only ribosomes working at mitochondria.

    The researchers then used a method originally developed by the Weissman lab to extract the sections of RNA inside of the ribosomes. This allows them to see exactly how far along in the process of making a protein the ribosome is when captured, which can reveal whether the entire protein is made at the mitochondria, or whether it is partly produced elsewhere and only gets completed at the mitochondria.

    “One advantage of our tool is the granularity it provides,” Luo says. “Being able to see what section of the protein is locally translated helps us understand more about how localized translation is regulated, which can then allow us to understand its dysregulation in disease and to control localized translation in future studies.”

    Two protein groups are made at mitochondria

    Using these approaches, the researchers found that about 20 percent of the genes needed in mitochondria that are located in the main cellular genome are locally translated at mitochondria. These proteins can be divided into two distinct groups with different evolutionary histories and mechanisms for localized translation.

    One group consists of relatively long proteins, each containing more than 400 amino acids or protein building blocks. These proteins tend to be of bacterial origin — present in the ancestor of mitochondria — and they are locally translated in both mammalian and yeast cells, suggesting that their localized translation has been maintained through a long evolutionary history.

    Like many mitochondrial proteins encoded in the nucleus, these proteins contain a mitochondrial targeting sequence (MTS), a ZIP code that tells the cell where to bring them. The researchers discovered that most proteins containing an MTS also contain a nearby inhibitory sequence that prevents transportation until they are done being made. This group of locally translated proteins lacks the inhibitory sequence, so they are brought to the mitochondria during their production.

    Production of these longer proteins begins anywhere in the cell, and then after approximately the first 250 amino acids are made, they get transported to the mitochondria. While the rest of the protein gets made, it is simultaneously fed into a channel that brings it inside the mitochondrion. This ties up the channel for a long time, limiting import of other proteins, so cells can only afford to do this simultaneous production and import for select proteins. The researchers hypothesize that these bacterial-origin proteins are given priority as an ancient mechanism to ensure that they are accurately produced and placed within mitochondria.

    The second locally translated group consists of short proteins, each less than 200 amino acids long. These proteins are more recently evolved, and correspondingly, the researchers found that the mechanism for their localized translation is not shared by yeast. Their mitochondrial recruitment happens at the RNA level. Two sequences within regulatory sections of each RNA molecule that do not encode the final protein instead code for the cell’s machinery to recruit the RNAs to the mitochondria.

    The researchers searched for molecules that might be involved in this recruitment, and identified the RNA binding protein AKAP1, which exists at mitochondria. When they eliminated AKAP1, the short proteins were translated indiscriminately around the cell. This provided an opportunity to learn more about the effects of localized translation, by seeing what happens in its absence. When the short proteins were not locally translated, this led to the loss of various mitochondrial proteins, including those involved in oxidative phosphorylation, our cells’ main energy generation pathway.

    In future research, Weissman and Luo will delve deeper into how localized translation affects mitochondrial function and dysfunction in disease. The researchers also intend to use LOCL-TL to study localized translation in other cellular processes, including in relation to embryonic development, neural plasticity, and disease.

    “This approach should be broadly applicable to different cellular structures and cell types, providing many opportunities to understand how localized translation contributes to biological processes,” Weissman says. “We’re particularly interested in what we can learn about the roles it may play in diseases including neurodegeneration, cardiovascular diseases, and cancers.”

    Reference: Luo J, Khandwala S, Hu J, et al. Proximity-specific ribosome profiling reveals the logic of localized mitochondrial translation. Cell. 2025. doi: 10.1016/j.cell.2025.08.002

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  • UCL Study Recreates Early RNA–Amino Acid Link

    UCL Study Recreates Early RNA–Amino Acid Link

    Chemists at UCL have shown how two of biology’s most fundamental ingredients, RNA (ribonucleic acid) and amino acids, could have spontaneously joined together at the origin of life four billion years ago.

    Amino acids are the building blocks of proteins, the “workhorses” of life essential to nearly every living process. But proteins cannot replicate or produce themselves – they require instructions. These instructions are provided by RNA, a close chemical cousin of DNA (deoxyribonucleic acid).

    In a new study, published in Nature, researchers chemically linked life’s amino acids to RNA in conditions that could have occurred on the early Earth – an achievement that has eluded scientists since the early 1970s.

    Senior author Professor Matthew Powner, based at UCL’s Department of Chemistry, said: “Life relies on the ability to synthesise proteins – they are life’s key functional molecules. Understanding the origin of protein synthesis is fundamental to understanding where life came from.

    “Our study is a big step towards this goal, showing how RNA might have first come to control protein synthesis.

    “Life today uses an immensely complex molecular machine, the ribosome, to synthesise proteins. This machine requires chemical instructions written in messenger RNA, which carries a gene’s sequence from a cell’s DNA to the ribosome. The ribosome then, like a factory assembly line, reads this RNA and links together amino acids, one by one, to create a protein.

    “We have achieved the first part of that complex process, using very simple chemistry in water at neutral pH to link amino acids to RNA. The chemistry is spontaneous, selective and could have occurred on the early Earth.”

    Previous attempts to attach amino acids to RNA used highly reactive molecules, but these broke down in water and caused the amino acids to react with each other, rather than become linked to RNA.

    For the new study, the researchers took inspiration from biology, using a gentler method to convert life’s amino acids into a reactive form. This activation involved a thioester, a high-energy chemical compound important in many of life’s biochemical processes and that has already been theorised to play a role at the start of life*.

    Professor Powner said: “Our study unites two prominent origin of life theories – the ‘RNA world’, where self-replicating RNA is proposed to be fundamental, and the ‘thioester world’, in which thioesters are seen as the energy source for the earliest forms of life.”

    In order to form these thioesters, the amino acids react with a sulphur-bearing compound called pantetheine. Last year, the same team published a paper demonstrating pantetheine can be synthesised under early Earth-like conditions, suggesting it was likely to play a role in starting life.

    The next step, the researchers said, was to establish how RNA sequences could bind preferentially to specific amino acids, so that RNA could begin to code instructions for protein synthesis – the origin of the genetic code.

    “There are numerous problems to overcome before we can fully elucidate the origin of life, but the most challenging and exciting remains the origins of protein synthesis,” said Professor Powner.

    Lead author Dr Jyoti Singh, from UCL Chemistry, said: “Imagine the day that chemists might take simple, small molecules, consisting of carbon, nitrogen, hydrogen, oxygen, and sulphur atoms, and from these LEGO pieces form molecules capable of self-replication. This would be a monumental step towards solving the question of life’s origin.

    “Our study brings us closer to that goal by demonstrating how two primordial chemical LEGO pieces (activated amino acids and RNA) could have built peptides**, short chains of amino acids that are essential to life.

    “What is particularly groundbreaking is that the activated amino acid used in this study is a thioester, a type of molecule made from Coenzyme A, a chemical found in all living cells. This discovery could potentially link metabolism, the genetic code and protein building.”

    While the paper focuses solely on the chemistry, the research team said that the reactions they demonstrated could plausibly have taken place in pools or lakes of water on the early Earth (but not likely in the oceans as the concentrations of the chemicals would likely be too diluted).

    The reactions are too small to see with a visible-light microscope and were tracked using a range of techniques that are used to probe the structure of molecules, including several types of magnetic resonance imaging (which shows how the atoms are arranged) and mass spectrometry (which shows the size of molecules).

    Reference: Singh J, Thoma B, Whitaker D, Satterly Webley M, Yao Y, Powner MW. Thioester-mediated RNA aminoacylation and peptidyl-RNA synthesis in water. Nature. 2025;644(8078):933-944. doi: 10.1038/s41586-025-09388-y

    This article has been republished from the following materials. Note: material may have been edited for length and content. For further information, please contact the cited source. Our press release publishing policy can be accessed here.

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  • SpaceX Falcon 9 rocket launches Starlink satellites on record-breaking 30th flight

    SpaceX Falcon 9 rocket launches Starlink satellites on record-breaking 30th flight

    SpaceX has broken its rocket reuse record again, notching a nice round number in the process.

    A Falcon 9 rocket lifted off from NASA’s Kennedy Space Center in Florida on Thursday (Aug. 28) at 4:12 a.m. EDT (0812 GMT), carrying 28 of SpaceX’s Starlink internet satellites toward low Earth orbit (LEO).

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  • Characterization and therapeutic evaluation of the lytic bacteriophage ENP2309 against vancomycin-resistant Enterococcus faecalis infections in a mice model | Virology Journal

    Characterization and therapeutic evaluation of the lytic bacteriophage ENP2309 against vancomycin-resistant Enterococcus faecalis infections in a mice model | Virology Journal

    Phage isolation and purification

    This study utilized 19 strains of Enterococcus from the Key Laboratory of Animal Disease Pathogen Diagnosis and Green Prevention and Control Technology in Qinghai Province as host bacteria. Wastewater samples were collected from various yak farms in Xining city for phage isolation. The phage isolation methods used were previously described by Liu et al. [13], and the phage isolation and purification process was as follows:

    First, wastewater samples were sterilized by filtration through a 0.22 μm membrane filter (Millipore). The filtrate was then mixed with the host bacteria at a 1:1 ratio (v/v). The mixture was then plated using the double-layer agar method (the bottom layer was 1.5% agar-solidified Todd-Hewitt broth, and the top layer was THB medium containing 0.5% agar). After incubation at 37 ℃ overnight, the formation and morphology of phage plaques were observed. A single phage plaque was subsequently aseptically picked and suspended in sterile PBS at room temperature for 4 h to allow phage dissociation. This suspension was then mixed again with the host bacteria and replated using the double-layer agar method. After overnight incubation at 37 °C, single plaques were isolated. This purification process was repeated three times to ultimately obtain purified phage isolates.

    Host range

    Suspensions of distinct Enterococcus strains were spread onto double-layer agar plates and preincubated at 37 °C for 2 h to form bacterial lawns. Subsequently, 5 µL aliquots of phage solution were spotted onto the solidified agar surface. Following overnight incubation at 37 °C, lytic activity was evaluated by counting the infection classes (+ 4, + 3, +2, + 1, and 0) within the bacterial lawns (Table 1). The methods described by Fayez et al. [14] were subsequently followed, Enterococcus faecalis GZ25 was used as the indicator bacterium, the efficiency of plating (EOP) was calculated. The EOP is defined as the ratio of the lysis titre of the phage against different test strains to that against the indicator bacterium.

    Table 1 Scoring criteria for plaque Lysis activity

    Morphological observation

    The phage particles were sequentially concentrated using PEG 8000 (Sigma‒Aldrich) precipitation followed by CsCl density gradient centrifugation according to established protocols [15]. The purified phage suspension was adsorbed onto 400-mesh carbon-coated copper grids (Ted Pella, USA) and stained with 1% (w/v) phosphotungstic acid (SolarBio, Beijing, China) for 10 min at room temperature. The grids were air-dried and subsequently imaged using an HT7700 transmission electron microscope (Hitachi, Japan) at 80 kV.

    Temperature stability

    Phage ENP2309 suspensions were subjected to thermal stability testing through 1-hour incubation at incremental temperatures ranging from 10 °C to 80 °C (10 °C intervals). Following thermal treatment, residual phage viability was quantified via the double-layer agar method. All experimental conditions were evaluated through triplicate independent biological replicates.

    pH stability

    The pH of the SM buffer was adjusted to values ranging from 2 to 13 using concentrated hydrochloric acid or sodium hydroxide solution. A total of 100 µL of phage mixture was added to 900 µL of SM buffer at various pH values and allowed to stand at 37 °C for 1 h. The phage titres were determined using the double-layer method. All experimental conditions were evaluated through triplicate independent biological replicates.

    Optimal multiplicity of infection

    Serial dilutions of phage ENP2309 were combined with host bacterial cultures (OD600 = 0.6) under conditions of varying multiplicity of infection (MOI = 10− 5, 10− 4, 10− 3, 10− 2, 10− 1, 1, 10, 102, 103, 104, and 105). After 10 min adsorption at 37 °C, the unbound phages were removed by centrifugation (8,000 r/min, 10 min, 4°C). The bacterial pellets were resuspended in 10 mL of fresh THB broth and incubated at 37 °C, and 200 r/min for 4 h. Phage progeny production was quantified through the double-layer agar method, The experiment was performed in triplicate.

    One step growth

    In accordance with on the methods of Zurabov et al. [16], with adjustments made for this study, the following protocol was used: host bacterial cultures (OD600 = 0.6) were infected with phage ENP2309 at an MOI of 0.001. A mixture of 100 µL of phage suspension and 100 µL of host bacterial culture was incubated at 37 °C for 10 min. The mixture was then centrifuged (8,000 r/min, 5 min, 4 °C). The resulting pellet was collected and resuspended in 50 mL of THB broth. The mixture was incubated in a shaking incubator (37 °C, 200 rpm/min). Every 20 min, a 2 mL aliquot of the suspension was collected, and the phage suspension was obtained by filtration through a 0.22 μm filter. Phage titres were determined using the double-layer agar plate method, and monitored continuously for 6 h. The latent period was defined as the time required for phage adsorption to the host cell and subsequent release of progeny phages. The burst size of the phage was expressed as the ratio of the final count of phage particles released during the outburst to the number of infected bacterial cells. Burst size = (Peak phage titer) / (Total number of infected bacteria in the system). The experiment was performed in triplicate.

    Phage genome extraction and sequencing

    The phage genome was extracted using a bacteriophage DNA isolation kit (Norgen Biotek, Canada) following the manufacturer’s protocol. The purified DNA was quantified using a Nano Drop One (Thermo Fisher Scientific) and assessed for quality by agarose gel electrophoresis (1% w/v). Sequencing libraries were prepared using the Illumina TruSeq Nano DNA LT Library Prep Kit (Illumina, San Diego, CA) according to the manufacturer’s instructions (Illumina TruSeq DNA Sample Preparation Guide, Rev. E) at Shanghai Paisenno Bio-Tech Co., Ltd. Raw sequencing reads were quality-filtered using Trimmomatic (v0.39) and assembled de novo using SPAdes (v3.12.0) with default parameters. Contigs were screened on the basis of sequencing depth (> 50× coverage), and high-depth sequences were subjected to BLASTn analysis against the NCBI NT database [17] for phage genome identification. The final complete genome sequence was validated through manual curation and comparison with reference phage genomes in the NCBI database.

    Phage genome analysis

    The online BLASTp server was used to identify open reading frames (ORFs). The online tools ResFinder (http://genepi.food.dtu.dk/resfinder) and VirulenceFinder (https://cge.cbs.dtu.dk/services/) were used to screen for antibiotic resistance genes and virulence genes in the phage genome. tRNAs were predicted using tRNA scan SE (http://lowelab.ucsc.edu/tRNAscan-SE/index.html). A phage genome map was generated using SnapGene 6.0.2. To analyse the phylogenetic relationships of the phage, the genome sequence was used for a BLASTn search of the NCBI database. A phylogenetic tree based on the large terminase subunits of related phages was constructed by the neighbour‒joining method in MEGA 7.0 [18]. Phage genomes were compared using VIRIDIC [19] to determine their genetic relatedness (≥ 70% nucleotide sequence identity implies a genus-level relationship, whereas ≥ 95% identity suggests a species-level relationship).

    Evaluation of phage therapeutic effects

    Female BALB/C mice (16–18 g, purchased from the Lanzhou Institute of Animal Husbandry and Veterinary Medicine) were randomly allocated into four experimental groups (n = 10 per group): (a) Challenge group: Mice were intraperitoneally challenged with E. faecalis GZ16185 at the minimum lethal dose (3.0 × 10¹¹ CFU/mL). (b) Treatment group: 200 µL of phage ENP2309 (2.0 × 10⁸ PFU/mL) was administered via intraperitoneal injection 15 min post-infection. (c) Phage group: This group received 200 µL of phage ENP2309 alone (2.0 × 10⁸ PFU/mL) intraperitoneally. (d) PBS group: Injected intraperitoneally with 200 µL of PBS buffer.

    The experimental cycle spanned 14 days. Throughout the study, daily body weight, survival rates, and general health status were recorded for all groups.

    In addition to the mice in the challenge group (Day 3), the mice in the other groups were assessed at the endpoint (Day 14). The mice were euthanized, and the organs (e.g., liver, and spleen) were harvested for histopathological evaluation. Tissue sections were prepared and stained with haematoxylin-eosin (HE) to assess pathological changes. The bacterial loads in the spleen and liver were quantified using the plate counting method.

    Blood samples were collected via retro-orbital bleeding on Days1, 3, 5, and 7 posttreatment. Serum cytokine levels (e.g., TNF-α, IL-6 and IL-10) were quantified using commercial ELISA kits according to the manufacturers’ protocols.

    Statistical analysis

    All data were processed for statistical analysis (means and standard deviations) using SPSS 22.0, and graphical representations were generated using OriginPro 2021. Group differences were evaluated by one-way ANOVA, followed by Bonferroni correction. P values < 0.05 were considered statistically significant. Significance is indicated in the figures by asterisks (*, P < 0.05; **, P < 0.01; ***, P < 0.001).

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  • Spiders turn fireflies into glowing traps

    Spiders turn fireflies into glowing traps

    Ecologists have observed a species of nocturnal spider attracting prey to its web using the bioluminescent beacons of already trapped fireflies. This rare example of a predator exploiting its prey’s mating signal for its own gain is documented in the British Ecological Society’s Journal of Animal Ecology.

    Researchers at Tunghai University, Taiwan have observed sheet web spiders Psechrus clavis capturing fireflies in their webs and leaving them there while they emitted bioluminescent light for up to an hour. The researchers even observed the spiders going to check on the captured fireflies from time to time.

    Intrigued by this unusual behavior the researchers set up an experiment to test whether this was a strategy used by the spiders to increase their hunting success. In the experiment, they placed LEDs that resembled fireflies, in real sheet spider webs and left other webs clear as controls.

    They found three times the amount of prey was attracted to webs with the LEDs compared to the control webs. This increased to ten times more prey when they only looked at fireflies being captured.

    The findings confirm that captured fireflies left as bait increase the hunting success rate of the spiders. The researchers also noticed that the majority of captured fireflies were male, who were likely mistaking the glow for potential mates.

    Dr I-Min Tso, the lead author of the study said: “Our findings highlight a previously undocumented interaction where firefly signals, intended for sexual communication, are also beneficial to spiders.

    “This study sheds new light on the ways that nocturnal sit-and-wait predators can rise to the challenges of attracting prey and provides a unique perspective on the complexity of predator-prey interactions.”

    The researchers suggest that this behavior could have developed in sheet web spiders to avoid costly investment in their own bioluminescence like other sit-and-wait predators, such as anglerfish. Instead, the spiders are able to outsource prey attraction to their prey’s own signals.

    The sheet web spider Psechrus clavis is a nocturnal sit and wait predator found in subtropical forests of East Asia. It’s main source of prey, the winter firefly Diaphanes lampyroides, uses continuous, non-flashing bioluminescence to attract mates.

    Video footage captured by the researchers (see link below) in their experiment shows sheet web spiders employing different strategies when interacting with different prey species. Spiders would immediately consume any moths captured in their webs but would not immediately consume fireflies they captured.

    “Handling prey in different ways suggests that the spider can use some kind of cue to distinguish between the prey species they capture and determine an appropriate response.” explained Dr I-Min Tso. “We speculate that it is probably the bioluminescent signals of the fireflies that are used to identify fireflies enabling spiders to adjust their prey handling behavior accordingly.”

    The researchers conducted their field experiment in the conifer plantation forest at National Taiwan University’s Xitou Nature Educational Area.

    Because they used LEDs to mimic the light signal emitted by fireflies, the researchers warn that although the wavelength and intensity of the LED set up was a close match to fireflies, it would be best if real fireflies were used in the field experiment. But they admit that this would be extremely difficult in practice.

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  • Extremely stripped star reveals heavy elements as it explodes – Physics World

    Extremely stripped star reveals heavy elements as it explodes – Physics World






    Extremely stripped star reveals heavy elements as it explodes – Physics World


















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