Evidence map›Paper›PMID 32337752›Full record

ArticleThe EMBO journal2020

Bacterial rhomboid proteases mediate quality control of orphan membrane proteins.

Guangyu Liu, Stephen E Beaton, Adam G Grieve, Rhiannon Evans, Miranda Rogers, Kvido Strisovsky, Fraser A Armstrong, Matthew Freeman, Rachel M Exley, Christoph M Tang

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  4. Regulation of mixotrophy inMicrobiology (Reading, England) · 2026
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  18. Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Microorganisms · 2022
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Guangyu LiuSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Stephen E BeatonInorganic Chemistry Laboratory, University of Oxford, Oxford, UK.
Adam G GrieveSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Rhiannon EvansInorganic Chemistry Laboratory, University of Oxford, Oxford, UK.
Miranda RogersSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Kvido StrisovskyInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Praha 6, Czech Republic.ORCID 0000-0003-3677-0907
Fraser A ArmstrongInorganic Chemistry Laboratory, University of Oxford, Oxford, UK.
Matthew FreemanSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0003-0410-5451
Rachel M ExleySir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Christoph M TangSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0001-8366-3245
University of Oxford · GBCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZ

Funding

BBSRC BB/N006321/1Czech Academy of Sciences 61388963Czech Science Foundation 18-09556SDakota FoundationEPA ScholarshipERDF/ESF CZ.02.1.01/0.0/0.0/16_019/0000729Wellcome Trust 102908/Z/13/ZWellcome Trust (WT) 102908/Z/13/Z
6 · The paper itself

Abstract

Although multiprotein membrane complexes play crucial roles in bacterial physiology and virulence, the mechanisms governing their quality control remain incompletely understood. In particular, it is not known how unincorporated, orphan components of protein complexes are recognised and eliminated from membranes. Rhomboids, the most widespread and largest superfamily of intramembrane proteases, are known to play key roles in eukaryotes. In contrast, the function of prokaryotic rhomboids has remained enigmatic. Here, we show that the Shigella sonnei rhomboid proteases GlpG and the newly identified Rhom7 are involved in membrane protein quality control by specifically targeting components of respiratory complexes, with the metastable transmembrane domains (TMDs) of rhomboid substrates protected when they are incorporated into a functional complex. Initial cleavage by GlpG or Rhom7 allows subsequent degradation of the orphan substrate. Given the occurrence of this strategy in an evolutionary ancient organism and the presence of rhomboids in all domains of life, it is likely that this form of quality control also mediates critical events in eukaryotes and protects cells from the damaging effects of orphan proteins.

Indexed as

Bacterial ProteinsElectron TransportEndopeptidasesMembrane ProteinsProtein DomainsProteolysisShigella sonneiSubstrate SpecificityBacterial ProteinsEndopeptidasesMembrane Proteinsintramembrane proteolysismembrane protein complexesquality controlrhomboidShigella

Identifiers

PMID32337752
PMCPMC7232013
OpenAlexW3018272398

What OpenQuestion holds

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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.