Interplay between the Hsp90 Chaperone and the HslVU Protease To Regulate the Level of an Essential Protein in Shewanella oneidensis.
heat shock
proteases
protein chaperone
protein folding
proteostasis
stress adaptation
Journal
mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231
Informations de publication
Date de publication:
14 05 2019
14 05 2019
Historique:
entrez:
16
5
2019
pubmed:
16
5
2019
medline:
6
7
2019
Statut:
epublish
Résumé
Protein synthesis, folding, and degradation are an accurately regulated process occurring in every organism and called proteostasis. This process is essential to maintain a healthy proteome since proteostasis dysregulation is responsible for devastating cellular issues. Proteostasis is controlled by a complex network of molecular chaperones and proteases. Among them, eukaryotic Hsp90, assisted by many cochaperones and the Hsp70 chaperone system, plays a major role in activating hundreds of client proteins, and Hsp90 inhibition usually leads to proteasomal degradation of these clients. In bacteria, however, the precise function of Hsp90 remains quite unclear, and only a few clients are known. Recently, we have shown that Hsp90 is essential at elevated temperature in the aquatic model bacterium
Identifiants
pubmed: 31088919
pii: mBio.00269-19
doi: 10.1128/mBio.00269-19
pmc: PMC6520445
pii:
doi:
Substances chimiques
Bacterial Proteins
0
HSP70 Heat-Shock Proteins
0
HSP90 Heat-Shock Proteins
0
Proteome
0
Endopeptidase Clp
EC 3.4.21.92
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2019 Honoré et al.
Références
Nat Rev Mol Cell Biol. 2017 Jun;18(6):345-360
pubmed: 28429788
Annu Rev Biochem. 2011;80:587-612
pubmed: 21469952
J Biol Chem. 2014 Feb 28;289(9):6110-9
pubmed: 24415765
Proc Natl Acad Sci U S A. 2011 Dec 13;108(50):20136-41
pubmed: 22114197
Biochem Biophys Res Commun. 2010 Sep 17;400(2):241-5
pubmed: 20727857
Mol Microbiol. 2000 Jun;36(6):1360-70
pubmed: 10931286
Biochim Biophys Acta. 2012 Mar;1823(3):683-8
pubmed: 21871502
J Mol Biol. 2018 Sep 14;430(18 Pt B):3029-3040
pubmed: 29782836
Cell Rep. 2017 Apr 25;19(4):680-687
pubmed: 28445720
Subcell Biochem. 2015;78:219-42
pubmed: 25487024
Cell Stress Chaperones. 2015 Nov;20(6):951-7
pubmed: 26246199
FEBS Lett. 2010 Jan 21;584(2):272-7
pubmed: 19944692
Nature. 2009 Oct 22;461(7267):1144-8
pubmed: 19847269
Proc Natl Acad Sci U S A. 2011 May 17;108(20):8206-11
pubmed: 21525416
J Infect Dis. 2016 Sep 15;214(6):916-24
pubmed: 27412582
Mol Cell. 2015 Apr 2;58(1):8-20
pubmed: 25839432
Mol Cell. 2018 May 3;70(3):545-552.e9
pubmed: 29706537
Science. 2016 Jul 1;353(6294):aac4354
pubmed: 27365453
J Bacteriol. 1988 Jul;170(7):2977-83
pubmed: 3290192
PLoS Genet. 2013;9(7):e1003631
pubmed: 23874229
Mol Microbiol. 2010 May;76(3):576-89
pubmed: 20345653
Annu Rev Biochem. 2016 Jun 2;85:715-42
pubmed: 27050154
Biochim Biophys Acta. 2012 Mar;1823(3):607-13
pubmed: 22008467
Nat Rev Mol Cell Biol. 2010 Jul;11(7):515-28
pubmed: 20531426
J Biol Chem. 2019 Feb 8;294(6):2109-2120
pubmed: 30401745