The Hsp40 J‐domain modulates Hsp70 conformation and ATPase activity with a semi‐elliptical spring
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چکیده
منابع مشابه
The Hsp70 and Hsp40 chaperones influence microtubule stability in Chlamydomonas.
Mutations at the APM1 and APM2 loci in the green alga Chlamydomonas reinhardtii confer resistance to phosphorothioamidate and dinitroaniline herbicides. Genetic interactions between apm1 and apm2 mutations suggest an interaction between the gene products. We identified the APM1 and APM2 genes using a map-based cloning strategy. Genomic DNA fragments containing only the DNJ1 gene encoding a type...
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Networks of molecular chaperones maintain cellular protein homeostasis by acting at nearly every step in the biogenesis of proteins and protein complexes. Herein, we demonstrate that the major chaperone DnaK/HSP70 of the model bacterium Escherichia coli is critical for the proper functioning of the central metabolism and for the cellular response to carbon nutrition changes, either directly or ...
متن کاملBinding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in protein homeostasis. In these various tasks, the activity of Hsp70 is shaped by interactions with co-chaperones, such as Hsp40. The Hsp40 family of co-chaperones binds to Hsp70 through a conserved J-domain, and these factors stimulate ATPase and protein-folding activity. Using chemical screens, ...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2017
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.3223