J-Domain Proteins in Bacteria and Their Viruses.
Adenosine Triphosphatases
/ genetics
Bacteria
/ virology
Bacteriophages
/ genetics
Escherichia coli
/ genetics
Escherichia coli Proteins
/ genetics
HSP40 Heat-Shock Proteins
/ genetics
HSP70 Heat-Shock Proteins
/ genetics
Humans
Metabolic Networks and Pathways
/ genetics
Molecular Chaperones
/ genetics
Protein Biosynthesis
/ genetics
Protein Domains
/ genetics
CheY
HscA/HscC
NERD
PilZ
SNARE
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
12 06 2020
12 06 2020
Historique:
received:
06
03
2020
revised:
10
04
2020
accepted:
14
04
2020
pubmed:
20
4
2020
medline:
29
12
2020
entrez:
20
4
2020
Statut:
ppublish
Résumé
Molecular chaperones maintain cellular protein homeostasis by acting at almost every step in protein biogenesis pathways. The DnaK/HSP70 chaperone has been associated with almost every known essential chaperone functions in bacteria. To act as a bona fide chaperone, DnaK strictly relies on essential co-chaperone partners known as the J-domain proteins (JDPs, DnaJ, Hsp40), which preselect substrate proteins for DnaK, confer its specific cellular localization, and stimulate both its weak ATPase activity and substrate transfer. Remarkably, genome sequencing has revealed the presence of multiple JDP/DnaK chaperone/co-chaperone pairs in a number of bacterial genomes, suggesting that certain pairs have evolved toward more specific functions. In this review, we have used representative sets of bacterial and phage genomes to explore the distribution of JDP/DnaK pairs. Such analysis has revealed an unexpected reservoir of novel bacterial JDPs co-chaperones with very diverse and unexplored function that will be discussed.
Identifiants
pubmed: 32305462
pii: S0022-2836(20)30301-6
doi: 10.1016/j.jmb.2020.04.014
pii:
doi:
Substances chimiques
DNAJB1 protein, human
0
Escherichia coli Proteins
0
HSP40 Heat-Shock Proteins
0
HSP70 Heat-Shock Proteins
0
Molecular Chaperones
0
Adenosine Triphosphatases
EC 3.6.1.-
dnaK protein, E coli
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
3771-3789Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.