A bacteriophage-encoded J-domain protein interacts with the DnaK/Hsp70 chaperone and stabilizes the heat-shock factor σ32 of Escherichia coli.

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...

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Bibliographic Details
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

Internet

http://europepmc.org/articles/PMC3486835?pdf=render

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