| First Author | Ohno M | Year | 2004 |
| Journal | FEBS Lett | Volume | 576 |
| Issue | 3 | Pages | 381-6 |
| PubMed ID | 15498567 | Mgi Jnum | J:386781 |
| Mgi Id | MGI:8350018 | Doi | 10.1016/j.febslet.2004.09.044 |
| Citation | Ohno M, et al. (2004) Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity. FEBS Lett 576(3):381-6 |
| abstractText | 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 alpha-lactalbumin (RCMLA) as a substrate was used in gel filtration experiment, we observed the complex formation only for the truncation variants containing the long alpha-helix C in the helical lid. However, RCMLA binding occurred even for the variants lacking alpha-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. |
