Evidence map›Paper›PMID 42209473›Full record

ArticleNature communications2026

Structure of ergosteryl-aspartate synthase reveals how an entrapped tRNA is used like a prosthetic swinging arm in the synthesis of aminoacylated sterols.

Hanako Murayama, Nathaniel Yakobov, Nassira Mahmoudi, Sasha Legrosdidier, Nicolas Fournier, Solène Zuttion, Kanata Matsumoto, Michihiro Nishimura, Jingwei Ji, Bruno Senger and 10 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors.

Hanako Murayama *Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0009-0009-3026-5070
Nathaniel Yakobov *Génétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0001-9074-1651
Nassira MahmoudiGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.
Sasha LegrosdidierNanolive SA, Tolochenaz, Switzerland.
Nicolas FournierGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.
Solène ZuttionGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.
Kanata MatsumotoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Michihiro NishimuraDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-6182-8886
Jingwei JiDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Bruno SengerGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-5157-7307
Laurence HuckGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.
Howard B GamperDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, USA.ORCID 0000-0001-9007-8546
Yoshiaki KiseDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-1840-5028
Ralph E KleinerDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID 0000-0003-0508-9975
Mathieu FrechinNanolive SA, Tolochenaz, Switzerland.ORCID 0000-0002-2310-5230
Ya-Ming HouDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, USA.ORCID 0000-0001-6546-2597
Hubert D BeckerGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France.
Yuzuru ItohDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. yuzuru.itoh@bs.s.u-tokyo.ac.jp.ORCID 0000-0001-7802-5572
Frédéric FischerGénétique Moléculaire, Génomique, Microbiologie, UMR 7156, CNRS, Université de Strasbourg, Strasbourg, France. frfischer@unistra.fr.
Osamu NurekiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. nureki@bs.s.u-tokyo.ac.jp.ORCID 0000-0003-1813-7008

Funding

tRNA in codon usageR35GM134931 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2020 to 2025
$5.4M
Japan Agency for Medical Research and Development (AMED) JP223fa627001Japan Agency for Medical Research and Development (AMED) JP23ama121002Japan Agency for Medical Research and Development (AMED) JP23ama121012MEXT | JST | Core Research for Evolutional Science and Technology (CREST) JPMJCR20E2NIGMS NIH HHS R35 GM134931NIH HHS R35GM134931
6 · The paper itself

Abstract

Ergosteryl-3β-O-L-aspartate synthase (ErdS) catalyzes tRNA-dependent aspartylation of ergosterol, a lipid essential for fungal cell membrane integrity. However, the functional significance of ergosteryl-aspartate and the molecular mechanisms underlying its synthesis remain unclear. Here, we show that ErdS localization is highly dynamic and that Erg-Asp is required for proper hyphal growth, sporulation, and spore germination, and likely influences stress tolerance. The cryo-electron microscopy structure of ErdS revealed an unprecedented sterol-binding pocket. In addition, the structures in complex with a non-hydrolyzable Asp-N-tRNA

Indexed as

AminoacyltransferasesRNA, TransferSterolsAspartic AcidBinding SitesCatalytic DomainCryoelectron MicroscopyErgosterolHyphaeModels, MolecularSpores, FungalAminoacyltransferasesAspartic AcidErgosterolRNA, TransferSterols

Identifiers

PMID42209473
PMCPMC13219428

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LicenceCC BY-NC-ND
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.