Misselwitz B, et al. (1998) J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 2(5):593-603
Abstract: Proteins of the Hsp70 family of ATPases, such as BiP, function together with J proteins to bind polypeptides in numerous cellular processes. Using a solid phase binding assay, we demonstrate that a conserved segment of the J proteins, the J domain, catalytically activates BiP molecules to bind peptides in its immediate vicinity. The J domain interacts with the ATP form of BiP and stimulates hydrolysis resulting in the rapid trapping of peptides, which are then only slowly released upon nucleotide exchange. Activation by the J domain allows BiP to trap peptides or proteins that it would not bind on its own. These results explain why BiP and probably all other Hsp70s can interact with a wide range of substrates and suggest that the J partner primarily determines the substrate specificity of Hsp70s.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.||PubMed ID: 9844632|
Topics addressed in this paper
Number of different genes curated to this paper: 2
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