Substrate recognition of collagen-specific molecular chaperone HSP47. Structural requirements and binding regulation

Takaki Koide, Shinichi Asada, Kazuhiro Nagata

研究成果: Article

54 引用 (Scopus)

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Prior to secretion, procollagen molecules are correctly folded to triple helices in the endoplasmic reticulum (ER). HSP47 specifically associates with procollagen in the ER during its folding and/or modification processes and is thought to function as a collagen-specific molecular chaperone (Nagata, K. (1996) Trends Biochem. Sci. 21, 23-26). However, structural requirements for substrate recognition and regulation of the binding have not yet been elucidated. Here, we show that a typical collagen model sequence, (Pro-Pro- Gly)(n), possesses sufficient structural information required for recognition by HSP47. A structure-activity relationship study using synthetic analogs of (Pro-Pro-Gly)(n) has revealed the requirements in both chain length and primary structure for the interaction. The substrate recognition of HSP47 has also been shown to be similar but distinct from that of prolyl 4-hydroxylase, an ER resident enzyme. Further, it has shown that the interaction of HSP47 with the substrate peptides is abolished by prolyl 4-hydroxylation of the second Pro residues in Pro-Pro-Gly triplets and that the fully prolyl 4- hydroxylated peptide, (Pro-Hyp-Gly)(n), does not interact with HSP47. We thus have proposed a model in which HSP47 dissociates from procollagen during the process of prolyl 4-hydroxylation in the ER.

元の言語English
ページ(範囲)34523-34526
ページ数4
ジャーナルJournal of Biological Chemistry
274
発行部数49
DOI
出版物ステータスPublished - 1999 12 3
外部発表Yes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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