[HTML][HTML] The nucleotide exchange factors of Hsp70 molecular chaperones
A Bracher, J Verghese - Frontiers in molecular biosciences, 2015 - frontiersin.org
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 replacement of Hsp70-bound ADP with ATP.
Bacteria and organelles of bacterial origin have only one known NEF type for Hsp70, GrpE …
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 replacement of Hsp70-bound ADP with ATP.
Bacteria and organelles of bacterial origin have only one known NEF type for Hsp70, GrpE …
GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones
A Bracher, J Verghese - The Networking of Chaperones by Co …, 2015 - Springer
Molecular chaperones of the Hsp70 family are key components of the cellular protein folding
machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis
and release. The ATPase activity of Hsp70 is regulated by two main classes of
cochaperones: J-domain proteins stimulate ATPase hydrolysis by Hsp70, while nucleotide
exchange factors (NEF) facilitate its conversion from the ADP-bound to the ATP-bound state,
thus closing the chaperone folding cycle. Beginning with the discovery of the prototypical …
machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis
and release. The ATPase activity of Hsp70 is regulated by two main classes of
cochaperones: J-domain proteins stimulate ATPase hydrolysis by Hsp70, while nucleotide
exchange factors (NEF) facilitate its conversion from the ADP-bound to the ATP-bound state,
thus closing the chaperone folding cycle. Beginning with the discovery of the prototypical …