Evidence map›Paper›PMID 18689473›Full record

ArticleJournal of bacteriology2008

Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.

Lyle A Simmons, Alan D Grossman, Graham C Walker

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.1field-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

36 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Unique Structural Fold of LonBA Protease fromInternational journal of molecular sciences · 2022
    Article
  8. Review
  9. Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. TnApplied and environmental microbiology · 2020
    Article
  14. Review
  15. Article
  16. Roles for ClpXP in regulating the circadian clock inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. Article
  19. Functional Diversity of AAA+ Protease Complexes inFrontiers in molecular biosciences · 2017
    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.

Lyle A SimmonsDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Alan D Grossman
Graham C Walker
Massachusetts Institute of Technology · US

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ENGELWARD, BEVIN P. · 1985 to 2020
$25.6M
MUTAGENESIS AND REPAIR OF DNAR01CA021615 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WALKER, GRAHAM C · 1985 to 2019
$6.5M
QUORUM SENSING AND GENE EXPRESSION IN BACILLUS SUBTILISR01GM050895 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GROSSMAN, ALAN D · 1994 to 2017
$5.6M
DNA Mismatch Repair in Bacillus subtilisF32CA113124 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SIMMONS, LYLE · 2005 to 2007
$143k
NCI NIH HHS CA113124NCI NIH HHS CA21615-27NCI NIH HHS F32 CA113124NCI NIH HHS R01 CA021615NIEHS NIH HHS P30 ES002109NIGMS NIH HHS GM50895NIGMS NIH HHS R01 GM050895
6 · The paper itself

Abstract

Among other functions, ATP-dependent proteases degrade misfolded proteins and remove several key regulatory proteins necessary to activate stress responses. In Bacillus subtilis, ClpX, ClpE, and ClpC form homohexameric ATPases that couple to the ClpP peptidase. To understand where these peptidases and ATPases localize in living cells, each protein was fused to a fluorescent moiety. We found that ClpX-GFP (green fluorescent protein) and ClpP-GFP localized as focal assemblies in areas that were not occupied by the nucleoid. We found that the percentage of cells with ClpP-GFP foci increased following heat shock independently of protein synthesis. We determined that ClpE-YFP (yellow fluorescent protein) and ClpC-YFP formed foci coincident with nucleoid edges, usually near cell poles. Furthermore, we found that ClpQ-YFP (HslV) localized as small foci, usually positioned near the cell membrane. We found that ClpQ-YFP foci were dependent on the presence of the cognate hexameric ATPase ClpY (HslU). Moreover, we found that LonA-GFP is coincident with the nucleoid during normal growth and that LonA-GFP also localized to the forespore during development. We also investigated LonB-GFP and found that this protein localized to the forespore membrane early in development, followed by localization throughout the forespore later in development. Our comprehensive study has shown that in B. subtilis several ATP-fueled proteases occupy distinct subcellular locations. With these data, we suggest that substrate specificity could be determined, in part, by the spatial and temporal organization of proteases in vivo.

Indexed as

Adenosine TriphosphatasesBacillus subtilisBacterial ProteinsCell MembraneCytosolEndopeptidase ClpGreen Fluorescent ProteinsHeat-Shock ProteinsLuminescent ProteinsProtease LaRecombinant Fusion ProteinsSigma FactorAdenosine TriphosphatasesBacterial ProteinsClpC protein, BacteriaClpE protein, bacteriaEndopeptidase Clpenhanced green fluorescent proteinGreen Fluorescent ProteinsHeat-Shock ProteinslonB protein, bacillus subtilisLuminescent ProteinsProtease LaRecombinant Fusion ProteinsSigma Factoryellow fluorescent protein, Bacteria

Identifiers

PMID18689473
PMCPMC2566193
OpenAlexW2122061852

What OpenQuestion holds

Textmetadata
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.