Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen

EMBO Journal

Volumn 19, Issue 10, 2000, Pages 2204-2211

  Tasab, Mohammed ^a   Batten, Margaret R ^a   Bulleid, Neil J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Hsp47; Molecular chaperone; Procollagen; Protein folding

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 47; PROCOLLAGEN;

ANIMAL CELL; ARTICLE; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT;

ANIMALS; HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PROCOLLAGEN; PROTEIN BINDING; PROTEIN FOLDING; RABBITS; RECOMBINANT PROTEINS;

ANIMALIA; MAMMALIA;

EID: 0034657132     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.10.2204     Document Type: Article

References (33)

1. Bächinger, H.-P. and Davis, J.M. (1990) Sequence specific thermal stability of the collagen triple helix. Int. J. Biol. Macromol., 13, 152-156.
2. Bonfanti, L. et al. (1998) Procollagen traverses the Golgi stack without leaving the lumen of the cisternae: evidence for cisternal maturation. Cell, 95, 993-1003.
3. Bruckner, P. and Eikenberry, E.F. (1984) Procollagen is more stable in cellulo than in vitro. Eur. J. Biochem., 140, 397-399.
4. 1 and their characterisation with circular dichroism and ultracentrifugation. Helv. Chim. Acta, 58, 1276-1287.
5. Bulleid, N.J. (1996) Novel approach to study the initial events in the folding and assembly of procollagen. Sem. Cell Dev. Biol., 7, 667-672.
6. Bulleid, N.J., Wilson, R. and Lees, J.F. (1996) Type III procollagen assembly in semi-intact cells: chain association, nucleation and triple helix folding do not require formation of inter-chain disulfide bonds but triple helix nucleation does require hydroxylation. Biochem. J., 317, 195-202.
7. Bulleid, N.J., Dalley, J.A. and Lees, J.F. (1997) The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis. EMBO J., 16, 6694-6701.
8. Chessler, S.D. and Byers, P.H. (1993) BiP binds type I procollagen proα chains with mutations in the carboxy-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem., 268, 18226-18233.
9. Engel, J. and Prockop, D.J. (1991) The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Annu. Rev. Biophys. Chem., 20, 137-152.
10. Fitzgerald, J., Lamandé, S.R. and Bateman, J.F. (1999) Proteosomal degradation of unassembled mutant type I collagen proα1(I) chains. J. Biol. Chem., 274, 27392-27398.
11. Gurevich, V.V., Pokrovskaya, I.D., Obukhova, T.A. and Zozulya, S.A. (1987) Preparative in vitro mRNA synthesis using SP6 and T7 polymerases. Anal. Biochem., 195, 207-213.
12. Hammond, C. and Helenius, A. (1995) Quality control in the secretory pathway. Curr. Opin. Cell Biol., 7, 523-529.
13. Hosakawa, N. and Nagata, K. (2000) Procollagen binds to both prolyl 4-hydroxylase/protein disulphide isomerase and Hsp47 within the endoplasmic reticulum in the absence of ascorbate. FEBS Lett., 466, 19-25.
14. John, D.C.A., Grant, M.E.G. and Bulleid, N.J. (1993) Cell-free synthesis and assembly of prolyl-4-hydroxylase: Association of the α-subunit with the β-subunit (PDI) prevents its misfolding and aggregation. EMBO J., 12, 1587-1595.
15. Juva, K. and Prockop, D.J. (1969) Formation of enzyme-substrate complexes with protocollagen proline hydroxylase and large polypeptide substrates. J. Biol. Chem., 23, 6486-6492.
16. Kadler, K. (1994) Fibril forming collagens. In Sheterline, P., (ed.), Protein Profiles: Extracellular Matrix I: Academic Press, Oxford, UK.
17. Kivirikko, K.I., Myllylä, R. and Pihlajaniemi, T. (1992) Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In Harding, J.J. and Crabbe, J.C. (eds), Post-translational Modification of Proteins. CRC Press, Boca Raton, FL, USA, pp. 1-51.
18. Koide, T., Asada, S. and Nagata, K. (1999) Substrate recognition of collagen-specific molecular chaperone HSP47. J. Biol. Chem., 274, 34523-34526.
19. Lamandé, S.H., Chessler, S.D., Golub, S.B., Byers, P.H., Chan, D., Cole, W.G., Sillence, D.O. and Bateman, J.F. (1995) Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the proα1(I) chain carboxy-terminal propeptide which impair subunit assembly. J. Biol. Chem., 270, 8642-8649.
20. Lees, J.F. and Bulleid, N.J. (1994) The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen. J. Biol. Chem., 269, 24354-24360.
21. Lees, J.F., Tasab, M. and Bulleid, N.J. (1997) Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen. EMBO J., 16, 908-916.
22. Leitzgen, K. and Haas, I.G. (1998) Protein maturation in the endoplasmic reticulum. Chemtracts Biochem. Mol. Biol., 11, 423-445.
23. McLaughlin, S.H. and Bulleid, N.J. (1998) Molecular recognition in procollagen chain assembly. Matrix Biol., 16, 369-377.
24. Nagata, K. (1996) Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci., 21, 23-26.
25. Nakai, A., Satoh, M., Hirayoshi, K. and Nagata, K. (1992) Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. J. Cell Biol., 117, 903-914.
26. Natsume, T., Koide, T., Yokota, S., Hirayoshi, K. and Nagata, K. (1994) Interactions between collagen-binding stress protein Hsp47 and collagen: analysis of kinetic parameters by surface plasmon resonance biosensor. J. Biol. Chem., 269, 31224-31228.
27. Ryhänen, L., Zaragoza, E.J. and Uitto, J. (1983) Conformational stability of type 1 collagen triple helix: evidence for temporary and local relaxation of the protein conformation using a proteolytic probe. Arch. Biochem. Biophys., 223, 562-571.
28. Satoh, M., Hirayoshi, K., Yokota, S.-I. Hosokawa, N and Nagata, K. (1996) Intracelluar interaction of collagen-specific stress protein HSP47 with newly synthesised procollagen. J. Cell Biol., 133, 469-483.
29. Sauk, J.J., Smith, T., Norris, K. and Ferreira, L. (1994) Hsp47 and the translocation-translocation machinery co-operate in the production of αI(I) chains of procollagen. J. Biol. Chem., 269, 3941-3946.
30. Uitto, J. (1979) Collagen polymorphism: isolation and partial characterisation of α1(I)-trimer molecules in normal human skin. Arch. Biochem. Biophys., 192, 371-379.
31. Walmsley, A.R., Batten, M.R., Lad, U. and Bulleid, N.J. (1999) Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase. J. Biol. Chem., 274, 14884-14892.
32. Wilson, R., Allen, A.J., Oliver, J., Brookman, J.L., High, S. and Bulleid, N.J. (1995) Development of a semi-permeabilised cell system to study the translocation, folding, assembly and transport of secretory proteins. Biochem. J., 307, 679-687.
33. Wilson, R., Lees, J.F. and Bulleid, N.J. (1998) Protein disulphide isomerase acts as a molecular chaperone during the assembly of procollagen. J. Biol. Chem., 273, 9637-9643.