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Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
576
Issue
3
Identifiers
DOI: 10.1016/j.febslet.2004.09.044
Keywords
  • C-Terminal Helical Lid
  • Heat Shock Protein 70
  • Peptide Binding
  • Substrate Mass
  • Truncation Variant
Disciplines
  • Biology

Abstract

Abstract Here, we produced the C-terminal truncation variants of mouse inducible heat shock protein 72 (Hsp72) to elucidate the regulatory role of the C-terminal helical lid of Hsp70 for substrate recognition. All of the truncation variants containing the substrate binding domain bound a short-length peptide substrate CLLLSAPRR. When a large mass reduced carboxymethyl α-lactalbumin (RCMLA) as a substrate was used in gel filtration experiment, we observed the complex formation only for the truncation variants containing the long α-helix C in the helical lid. However, RCMLA binding occurred even for the variants lacking α-helix C when their C-terminal region was anchored onto a solid phase. Together with the finding that helix C is involved in the self-association of Hsp70, our present data suggest that the C-terminal region of Hsp70 modulates the substrate recognition and its kinetics may be substrate-mass dependent.

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