Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain.
The 70-kilodalton heat shock protein (hsp70) family members appear to be essential components in a number cellular protein-protein interactions. We report here on the characterization of a new functional region in hsp70, a calmodulin-binding site. We have identified a 21-amino-acid sequence within the hsp70 protein that contains a calmodulin-binding domain. The peptide formed a potential amphipathic alpha helix and bound calmodulin with high affinity. Comparison of amino acid homology of this calmodulin-binding sequence with analogous hsp70 sequences from other species showed a high degree of conservation.
Stevenson
M A
MA
Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
Calderwood
S K
SK
D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D001681:Biological Assay; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D006360:Heat-Shock Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D051379:Mice; D008969:Molecular Sequence Data; D005810:Multigene Family; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism
D002147:Calmodulin; D006360:Heat-Shock Proteins; D009842:Oligopeptides; D010727:Phosphoric Diester Hydrolases; D002118:Calcium