Evidence map›Paper›PMID 26447507›Full record

ArticleeLife2015

Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage.

Koichiro Akiyama, Shinya Mizuno, Yohei Hizukuri, Hiroyuki Mori, Terukazu Nogi, Yoshinori Akiyama

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Inhibitory proteins ofJournal of bacteriology · 2025
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  4. Bacterial SEAL domains undergo autoproteolysis and function in regulated intramembrane proteolysis.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  8. Review
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  15. mBio · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Inhibitor of intramembrane protease RseP blocks the σProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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

6 authors.

Koichiro AkiyamaInstitute for Virus Research, Kyoto University, Kyoto, Japan.
Shinya MizunoInstitute for Virus Research, Kyoto University, Kyoto, Japan.
Yohei HizukuriInstitute for Virus Research, Kyoto University, Kyoto, Japan.
Hiroyuki MoriInstitute for Virus Research, Kyoto University, Kyoto, Japan.
Terukazu NogiGraduate School of Medical Life Science, Yokohama City University, Yokohama, Japan.
Yoshinori AkiyamaInstitute for Virus Research, Kyoto University, Kyoto, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular mechanisms underlying substrate recognition and cleavage by Escherichia coli RseP, which belongs to S2P family of intramembrane-cleaving proteases, remain unclear. We examined the function of a conserved region looped into the membrane domain of RseP to form a β-hairpin-like structure near its active site in substrate recognition and cleavage. We observed that mutations disturbing the possible β-strand conformation of the loop impaired RseP proteolytic activity and that some of these mutations resulted in the differential cleavage of different substrates. Co-immunoprecipitation and crosslinking experiments suggest that the loop directly interacts with the transmembrane segments of substrates. Helix-destabilising mutations in the transmembrane segments of substrates suppressed the effect of loop mutations in an allele-specific manner. These results suggest that the loop promotes substrate cleavage by selectively recognising the transmembrane segments of substrates in an extended conformation and by presenting them to the proteolytic active site, which contributes to substrate discrimination.

Indexed as

DNA Mutational AnalysisEndopeptidasesEscherichia coliEscherichia coli ProteinsImmunoprecipitationMembrane ProteinsModels, BiologicalModels, MolecularMutant ProteinsProtein Interaction MappingProtein Structure, TertiarySubstrate SpecificityEndopeptidasesEscherichia coli ProteinsMembrane ProteinsMutant ProteinsRseP protein, E colibiochemistrycell biologyE. coliextracytoplasmic stress responsehelix-destabilizing residueregulated intramembrane proteolysisRpoEsmall membrane protein

Identifiers

PMID26447507
PMCPMC4597795

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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.