Specific recognition of the collagen triple helix by chaperone HSP47

II. The HSP47-binding structural motif in collagens and related proteins

Takaki Koide, Yoshimi Nishikawa, Shinichi Asada, Chisato M. Yamazaki, Yoshifumi Takahara, Daisuke L. Homma, Akira Otaka, Katsuki Ohtani, Nobutaka Wakamiya, Kazuhiro Nagata, Kouki Kitagawa

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

The endoplasmic reticulum-resident chaperone heat-shock protein 47 (HSP47) plays an essential role in procollagen biosynthesis. The function of HSP47 relies on its specific interaction with correctly folded triple-helical regions comprised of Gly-Xaa-Yaa repeats, and Arg residues at Yaa positions have been shown to be important for this interaction. The amino acid at the Yaa position (Yaa-3) in the N-terminal-adjoining triplet containing the critical Arg (defined as Arg0) was also suggested to be directly recognized by HSP47 (Koide, T., Asada, S., Takahara, Y., Nishikawa, Y., Nagata, K., and Kitagawa, K. (2006) J. Biol. Chem. 281, 3432-3438). Based on this finding, we examined the relationship between the structure of Yaa-3 and HSP47 binding using synthetic collagenous peptides. The results obtained indicated that the structure of Yaa-3 determined the binding affinity for HSP47. Maximal binding was observed when Yaa-3 was Thr. Moreover, the required relative spatial arrangement of these key residues in the triple helix was analyzed by taking advantage of heterotrimeric collagen-model peptides, each of which contains one Thr-3 and one Arg0. The results revealed that HSP47 recognizes the Yaa-3 and Arg0 residues only when they are on the same peptide strand. Taken together, the data obtained led us to define the HSP47-binding structural epitope in the collagen triple helix and also define the HSP47-binding motif in the primary structure. A motif search against human protein database predicted candidate clients for this molecular chaperone. The search result indicated that not all collagen family proteins require the chaperoning by HSP47.

Original languageEnglish
Pages (from-to)11177-11185
Number of pages9
JournalJournal of Biological Chemistry
Volume281
Issue number16
DOIs
Publication statusPublished - 2006 Apr 21
Externally publishedYes

Fingerprint

HSP47 Heat-Shock Proteins
Protein Binding
Collagen
Proteins
Peptides
Procollagen
Protein Databases
Molecular Chaperones
Biosynthesis
Endoplasmic Reticulum
Epitopes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Specific recognition of the collagen triple helix by chaperone HSP47 : II. The HSP47-binding structural motif in collagens and related proteins. / Koide, Takaki; Nishikawa, Yoshimi; Asada, Shinichi; Yamazaki, Chisato M.; Takahara, Yoshifumi; Homma, Daisuke L.; Otaka, Akira; Ohtani, Katsuki; Wakamiya, Nobutaka; Nagata, Kazuhiro; Kitagawa, Kouki.

In: Journal of Biological Chemistry, Vol. 281, No. 16, 21.04.2006, p. 11177-11185.

Research output: Contribution to journalArticle

Koide, T, Nishikawa, Y, Asada, S, Yamazaki, CM, Takahara, Y, Homma, DL, Otaka, A, Ohtani, K, Wakamiya, N, Nagata, K & Kitagawa, K 2006, 'Specific recognition of the collagen triple helix by chaperone HSP47: II. The HSP47-binding structural motif in collagens and related proteins', Journal of Biological Chemistry, vol. 281, no. 16, pp. 11177-11185. https://doi.org/10.1074/jbc.M601369200
Koide, Takaki ; Nishikawa, Yoshimi ; Asada, Shinichi ; Yamazaki, Chisato M. ; Takahara, Yoshifumi ; Homma, Daisuke L. ; Otaka, Akira ; Ohtani, Katsuki ; Wakamiya, Nobutaka ; Nagata, Kazuhiro ; Kitagawa, Kouki. / Specific recognition of the collagen triple helix by chaperone HSP47 : II. The HSP47-binding structural motif in collagens and related proteins. In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 16. pp. 11177-11185.
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