Evidence map›Paper›PMID 18786145›Full record

ArticleMolecular microbiology2008

Localization of general and regulatory proteolysis in Bacillus subtilis cells.

Janine Kirstein, Henrik Strahl, Noël Molière, Leendert W Hamoen, Kürşad Turgay

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022
    Review
  5. Article
  6. Review
  7. Review
  8. TnApplied and environmental microbiology · 2020
    Article
  9. Protein aggregation in bacteria.FEMS microbiology reviews · 2020
    Review
  10. Article
  11. Functional Diversity of AAA+ Protease Complexes inFrontiers in molecular biosciences · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014
    Review
  18. Article
  19. Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  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

5 authors at 1 institution in 1 country.

Janine KirsteinInstitut für Biologie - Mikrobiologie, FU Berlin, Berlin, Germany.
Henrik Strahl
Noël Molière
Leendert W Hamoen
Kürşad Turgay
In-Q-Tel · US

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

Protein degradation mediated by ATP-dependent proteases, such as Hsp100/Clp and related AAA+ proteins, plays an important role in cellular protein homeostasis, protein quality control and the regulation of, e.g. heat shock adaptation and other cellular differentiation processes. ClpCP with its adaptor proteins and other related proteases, such as ClpXP or ClpEP of Bacillus subtilis, are involved in general and regulatory proteolysis. To determine if proteolysis occurs at specific locations in B. subtilis cells, we analysed the subcellular distribution of the Clp system together with adaptor and general and regulatory substrate proteins, under different environmental conditions. We can demonstrate that the ATPase and the proteolytic subunit of the Clp proteases, as well as the adaptor or substrate proteins, form visible foci, representing active protease clusters localized to the polar and to the mid-cell region. These clusters could represent a compartmentalized place for protein degradation positioned at the pole close to where most of the cellular protein biosynthesis and also protein quality control are taking place, thereby spatially separating protein synthesis and degradation.

Indexed as

Adenosine TriphosphatasesBacillus subtilisBacterial ProteinsCell DivisionEndopeptidase ClpHeat-Shock ProteinsHeat-Shock ResponseMicroscopy, FluorescenceRecombinant Fusion ProteinsTime FactorsAdenosine TriphosphatasesBacterial ProteinsEndopeptidase ClpHeat-Shock ProteinsRecombinant Fusion Proteins

Identifiers

PMID18786145
PMCPMC2628427
OpenAlexW2107586596

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.