A bacteriophage-encoded J-domain protein interacts with the DnaK/Hsp70 chaperone and stabilizes the heat-shock factor σ32 of Escherichia coli.
The universally conserved J-domain proteins (JDPs) are obligate cochaperone partners of the Hsp70 (DnaK) chaperone. They stimulate Hsp70's ATPase activity, facilitate substrate delivery, and confer specific cellular localization to Hsp70. In this work, we have identified and characterized the f...
Main Authors: | Elsa Perrody, Anne-Marie Cirinesi, Carine Desplats, France Keppel, Françoise Schwager, Samuel Tranier, Costa Georgopoulos, Pierre Genevaux |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2012-01-01
|
Series: | PLoS Genetics |
Online Access: | http://europepmc.org/articles/PMC3486835?pdf=render |
Similar Items
-
Impact of the molecular chaperone HSP70/DnaK on the Escherichia coli central metabolism
by: Anglès, Frédéric
Published: (2015) -
Understanding the allosteric mechanism of the Escherichia coli Hsp70 molecular chaperone, DnaK
by: Sivendran, Renuka
Published: (2004) -
Protein polarization driven by nucleoid exclusion of DnaK(HSP70)–substrate complexes
by: Clémence Collet, et al.
Published: (2018-05-01) -
Crystallographic Studies of the Hsp70 Chaperone System: Insight into the DnaK and GrpE Intermolecular Interaction
by: Chih-Chuang Wu, et al.
Published: (2012) -
How the E. Coli Hsp70 Molecular Chaperone, DnaK, Binds a Client Protein
by: Tilitsky, Joseph
Published: (2017)