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J. Biol. Chem., Vol. 281, Issue 16, 11177-11185, April 21, 2006

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Specific Recognition of the Collagen Triple Helix by Chaperone HSP47

II. THE HSP47-BINDING STRUCTURAL MOTIF IN COLLAGENS AND RELATED PROTEINS^*

Takaki Koide¹, Yoshimi Nishikawa², Shinichi Asada², Chisato M. Yamazaki, Yoshifumi Takahara, Daisuke L. Homma, Akira Otaka^¶, Katsuki Ohtani^||, Nobutaka Wakamiya^||, Kazuhiro Nagata^**, and Kouki Kitagawa

From the Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences, Niigata 956-8603, Japan, the Faculty of Engineering, The University of Tokushima, Tokushima 770-8506, Japan, the ^¶Graduate School of Pharmaceutical Science, The University of Tokushima, Tokushima 770-8505, Japan, the ^||Department of Microbiology, Asahikawa Medical College, Asahikawa 078-8510, Japan, and the ^**Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8397, Japan

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.

Received for publication, February 13, 2006

^* This work was supported by Grants-in-aid for Scientific Research in Priority Areas (No. 17028051) and the Encouragement of Young Scientists (No. 16689004) from MEXT, Japan, and by the Takeda Science Foundation. This is paper II in the series "Specific Recognition of the Collagen Triple Helix by Chaperone HSP47." Ref. 8 is paper I in this series. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Experimental Procedures, Fig. S1, and Table S1.

² These authors contributed equally to this work.

¹ To whom correspondence should be addressed. Tel.: 81-250-25-5255; Fax: 81-250-25-5255; E-mail: koi{at}niigata-pharm.ac.jp.

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