Evidence map›Paper›PMID 34931064›Full record

ArticleNature chemical biology2022

A counter-enzyme complex regulates glutamate metabolism in Bacillus subtilis.

Vijay Jayaraman, D John Lee, Nadav Elad, Shay Vimer, Michal Sharon, James S Fraser, Dan S Tawfik

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
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

13 citing papers in PubMed, 32 citations in OpenAlex.

  1. A cloaked glutamate decarboxylase sustains the GABA shunt inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  6. From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025
    Review
  7. Article
  8. Article
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  12. Review
  13. Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Vijay JayaramanDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel. vijay.jayaraman@weizmann.ac.il.ORCID http://orcid.org/0000-0001-6288-1841
D John Lee *Department of Bioengineering and Therapeutic Sciences, University of California San Francisco, San Francisco, CA, USA.
Nadav Elad *Department of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel.
Shay VimerDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.ORCID http://orcid.org/0000-0002-2289-6333
Michal SharonDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.ORCID http://orcid.org/0000-0003-3933-0595
James S FraserDepartment of Bioengineering and Therapeutic Sciences, University of California San Francisco, San Francisco, CA, USA. jfraser@fraserlab.com.ORCID http://orcid.org/0000-0002-5080-2859
Dan S TawfikDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
Weizmann Institute of Science · ILUniversity of California, San Francisco · US

Funding

Supplement to Resolving ensemble averaged conformations by multi-temperature x-ray crystallography - Equipment 2020R01GM123159 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2018 to 2021
$2.3M
CryoEM guided enhancement of ribosome-targeting antibioticsF32AI148120 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LEE, DAVID JOHN · 2019 to 2021
$135k
NIAID NIH HHS F32 AI148120NIGMS NIH HHS R01 GM123159
6 · The paper itself

Abstract

Multi-enzyme assemblies composed of metabolic enzymes catalyzing sequential reactions are being increasingly studied. Here, we report the discovery of a 1.6 megadalton multi-enzyme complex from Bacillus subtilis composed of two enzymes catalyzing opposite ('counter-enzymes') rather than sequential reactions: glutamate synthase (GltAB) and glutamate dehydrogenase (GudB), which make and break glutamate, respectively. In vivo and in vitro studies show that the primary role of complex formation is to inhibit the activity of GudB. Using cryo-electron microscopy, we elucidated the structure of the complex and the molecular basis of inhibition of GudB by GltAB. The complex exhibits unusual oscillatory progress curves and is necessary for both planktonic growth, in glutamate-limiting conditions, and for biofilm growth, in glutamate-rich media. The regulation of a key metabolic enzyme by complexing with its counter enzyme may thus enable cell growth under fluctuating glutamate concentrations.

Indexed as

Bacillus subtilisBacterial ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGlutamate DehydrogenaseGlutamate SynthaseGlutamic AcidBacterial ProteinsGlutamate DehydrogenaseGlutamate SynthaseGlutamic Acid

Identifiers

PMID34931064
PMCPMC8810680
OpenAlexW4225650071

What OpenQuestion holds

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Registered trials

None linked

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.