Hsp70 chaperones: Cellular functions and molecular mechanism
نویسندگان
چکیده
منابع مشابه
Functional specificity among Hsp70 molecular chaperones.
Molecular chaperones of the 70-kilodalton heat shock protein (Hsp70) class bind to partially unfolded polypeptide substrates and participate in a wide variety of cellular processes. Differences in peptide-binding specificity among Hsp70s have led to the hypothesis that peptide binding determines specific Hsp70 functions. Protein domains were identified that were required for two separate functi...
متن کاملCommon and divergent peptide binding specificities of hsp70 molecular chaperones.
We have studied the binding of synthetic peptides to three hsp70 molecular chaperones, DnaK, BiP, and hsc70, as a model for the interaction of hsp70 proteins with unfolded regions of target polypeptides. We measured the ability of 53 peptides to inhibit the formation of complexes between the hsp70 proteins and denatured lactalbumin. Peptides that bound with highest affinity to all three hsp70 p...
متن کاملMechanism of regulation of hsp70 chaperones by DnaJ cochaperones.
Hsp70 chaperones assist a large variety of protein folding processes within the entire lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ cochaperones. DnaJ stimulates Hsp70 to hydrolyze ATP, a key step that closes its substrate-binding cavity and thus allows stable binding of substrate. We show that DnaJ stimulates ATP hydrolysis by Escherichia coli Hsp70, Dna...
متن کاملAn interdomain sector mediating allostery in Hsp70 molecular chaperones
Allosteric coupling between protein domains is fundamental to many cellular processes. For example, Hsp70 molecular chaperones use ATP binding by their actin-like N-terminal ATPase domain to control substrate interactions in their C-terminal substrate-binding domain, a reaction that is critical for protein folding in cells. Here, we generalize the statistical coupling analysis to simultaneously...
متن کاملThe nucleotide exchange factors of Hsp70 molecular chaperones
Molecular chaperones of the Hsp70 family form an important hub in the cellular protein folding networks in bacteria and eukaryotes, connecting translation with the downstream machineries of protein folding and degradation. The Hsp70 folding cycle is driven by two types of cochaperones: J-domain proteins stimulate ATP hydrolysis by Hsp70, while nucleotide exchange factors (NEFs) promote replacem...
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ژورنال
عنوان ژورنال: Cellular and Molecular Life Sciences
سال: 2005
ISSN: 1420-682X,1420-9071
DOI: 10.1007/s00018-004-4464-6