Evidence map›Paper›PMID 36455053›Full record

ArticlePLoS biology2022

Inorganic sulfur fixation via a new homocysteine synthase allows yeast cells to cooperatively compensate for methionine auxotrophy.

Jason S L Yu, Benjamin M Heineike, Johannes Hartl, Simran K Aulakh, Clara Correia-Melo, Andrea Lehmann, Oliver Lemke, Federica Agostini, Cory T Lee, Vadim Demichev and 3 more

Abstract read
In one paragraph

Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
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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

13 authors.

Jason S L YuMolecular Biology of Metabolism Laboratory, The Francis Crick Institute, London, United Kingdom.
Benjamin M HeineikeMolecular Biology of Metabolism Laboratory, The Francis Crick Institute, London, United Kingdom.
Johannes HartlDepartment of Biochemistry, Charité Universitätsmedizin, Berlin, Germany.
Simran K AulakhMolecular Biology of Metabolism Laboratory, The Francis Crick Institute, London, United Kingdom.
Clara Correia-MeloMolecular Biology of Metabolism Laboratory, The Francis Crick Institute, London, United Kingdom.
Andrea LehmannDepartment of Biochemistry, Charité Universitätsmedizin, Berlin, Germany.
Oliver LemkeDepartment of Biochemistry, Charité Universitätsmedizin, Berlin, Germany.
Federica AgostiniDepartment of Biochemistry, Charité Universitätsmedizin, Berlin, Germany.
Cory T LeeDepartment of Biochemistry, Charité Universitätsmedizin, Berlin, Germany.
Vadim DemichevDepartment of Biochemistry, Charité Universitätsmedizin, Berlin, Germany.
Christoph B MessnerMolecular Biology of Metabolism Laboratory, The Francis Crick Institute, London, United Kingdom.
Michael MüllederCore Facility-High Throughput Mass Spectrometry, Charité Universitätsmedizin, Berlin, Germany.
Markus RalserMolecular Biology of Metabolism Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID 0000-0001-9535-7413

Funding

Cancer Research UK FC001134Medical Research Council FC001134Wellcome Trust 200829/Z/16/ZWellcome Trust FC001134
6 · The paper itself

Abstract

The assimilation, incorporation, and metabolism of sulfur is a fundamental process across all domains of life, yet how cells deal with varying sulfur availability is not well understood. We studied an unresolved conundrum of sulfur fixation in yeast, in which organosulfur auxotrophy caused by deletion of the homocysteine synthase Met17p is overcome when cells are inoculated at high cell density. In combining the use of self-establishing metabolically cooperating (SeMeCo) communities with proteomic, genetic, and biochemical approaches, we discovered an uncharacterized gene product YLL058Wp, herein named Hydrogen Sulfide Utilizing-1 (HSU1). Hsu1p acts as a homocysteine synthase and allows the cells to substitute for Met17p by reassimilating hydrosulfide ions leaked from met17Δ cells into O-acetyl-homoserine and forming homocysteine. Our results show that cells can cooperate to achieve sulfur fixation, indicating that the collective properties of microbial communities facilitate their basic metabolic capacity to overcome sulfur limitation.

Indexed as

Cysteine SynthaseMethionineSaccharomyces cerevisiaeCarbon-Oxygen LyasesCysteineProteomicsRacemethionineSaccharomyces cerevisiae ProteinsSulfurCarbon-Oxygen LyasesCysteineCysteine SynthaseMET17 protein, S cerevisiaeMethionineO-acetylhomoserine (thiol)-lyaseRacemethionineSaccharomyces cerevisiae ProteinsSulfurYLL058W protein, S cerevisiae

Identifiers

PMID36455053
PMCPMC9757880

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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.