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Role of the C‐terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity
Author(s) -
Ohno Michiko,
Kitabatake Naofumi,
Tani Fumito
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.044
Subject(s) - chaperone (clinical) , peptide , chemistry , terminal (telecommunication) , substrate specificity , microbiology and biotechnology , biochemistry , biophysics , biology , enzyme , computer science , medicine , telecommunications , pathology
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.