Evidence map›Paper›PMID 24942655›Full record

ArticleMolecular microbiology2014

Adaptor bypass mutations of Bacillus subtilis spx suggest a mechanism for YjbH-enhanced proteolysis of the regulator Spx by ClpXP.

Chio Mui Chan, Erik Hahn, Peter Zuber

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The Division Defect of aJournal of bacteriology · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. Protein aggregation in bacteria.FEMS microbiology reviews · 2020
    Review
  10. YjbH Solubility Controls Spx inFrontiers in microbiology · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018
    Review
  15. Article
  16. Article
  17. Review
  18. Functional Diversity of AAA+ Protease Complexes inFrontiers in molecular biosciences · 2017
    Review
  19. Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016
    Review
  20. 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

3 authors at 1 institution in 1 country.

Chio Mui ChanDivision of Environmental and Biomolecular Systems, Institute of Environmental Health, Oregon Health & Science University, Portland, OR, USA.
Erik Hahn
Peter Zuber
Oregon Health & Science University · US

Funding

Transcriptional Control by the Global Regulator SpxR01GM045898 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI ZUBER, PETER · 1992 to 2013
$4.2M
Characterization of YjbH: Insights into its role in oxidative stress responseF32GM099163 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI CHAN, CHIO MUI · 2012 to 2013
$106k
NIGMS NIH HHS F32 GM099163NIGMS NIH HHS F32GM099163NIGMS NIH HHS GM045898NIGMS NIH HHS R01 GM045898
6 · The paper itself

Abstract

The global regulator, Spx, is under proteolytic control exerted by the adaptor YjbH and ATP-dependent protease ClpXP in Bacillus subtilis. While YjbH is observed to bind the Spx C-terminus, YjbH shows little affinity for ClpXP, indicating adaptor activity that does not operate by tethering. Chimeric proteins derived from B. subtilis AbrB and the Spx C-terminus showed that a 28-residue C-terminal section of Spx (AbrB28), but not the last 12 or 16 residues (AbrB12, AbrB16), was required for YjbH interaction and for ClpXP proteolysis, although the rate of AbrB28 proteolysis was not affected by YjbH addition. The result suggested that the YjbH-targeted 28 residue segment of the Spx C-terminus bears a ClpXP-recognition element(s) that is hidden in the intact Spx protein. Residue substitutions in the conserved helix α6 of the C-terminal region generated Spx substrates that were degraded by ClpXP at accelerated rates compared to wild-type Spx, and showed reduced dependency on the YjbH activity. The residue substitutions also weakened the interaction between Spx and YjbH. The results suggest a model in which YjbH, through interaction with residues of helix α6, exposes the C-terminus of Spx for recognition and proteolysis by ClpXP.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceAmino Acid SubstitutionBacillus subtilisBacterial ProteinsEndopeptidase ClpMolecular Sequence DataMutationProteolysisSequence AlignmentBacterial ProteinsEndopeptidase Clp

Identifiers

PMID24942655
PMCPMC4128009
OpenAlexW2124025391

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.