Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen

EMBO Journal

Volumn 16, Issue 5, 1997, Pages 908-916

  Lees, Janice F ^a   Tasab, Mohammed ^a   Bulleid, Neil J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Chain selection; Molecular recognition; Procollagen

Indexed keywords

COLLAGEN TYPE 1; COLLAGEN TYPE 3; LEUCINE; METHIONINE; PROCOLLAGEN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BIOSYNTHESIS; CHIMERA; CONTROLLED STUDY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY;

AMINO ACID SEQUENCE; COLLAGENASES; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROCOLLAGEN; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

ANIMALIA;

EID: 0031055069     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.5.908     Document Type: Article

References (26)

1. Bachinger, H.P., Bruckner, P., Timpl, R., Prockop, D.J. and Engel, J. (1980) Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen: role of disulphide bridges and peptide bond isomerization. Eur. J. Biochem., 106, 619-632.
2. Bachinger, H.P., Fessler, L.I., Timpl, R. and Fessler, J.H. (1981) Chain assembly intermediate in the biosynthesis of type III procollagen in chick embryo blood vessels. J. Biol. Chem., 256, 13193-13199.
3. Brass, A., Kadler, K.E., Thomas, T., Grant, M.E. and Boot-Handford, R.P. (1992) The fibrillar collagens, collagenVII, collagenX and the C1q complement proteins share a similar domain in their C-terminal non-collagenous regions. FEBS Lett., 303, 126-128.
4. Bruckner, P. and Prockop, D.J. (1981) Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal. Biochem., 110, 360-368.
5. 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.
6. Cheah, K.S.E., Grant, M.E. and Jackson, D.S. (1979) Translation of type II procollagen mRNA and hydroxylation of the cell-free products. Biochem. Biophys. Res. Commun., 91, 1025-1031.
7. Chou, P.Y. and Fasman, G.D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol., 47, 45-148.
8. Dion, A.S. and Myers, J.C. (1987) COOH-terminal propeptides of the major human procollagens: Structural, functional and genetic comparisons. J. Mol. Biol., 193, 127-143.
9. Doege, K.J., and Fessler, J.H. (1986) Folding of carboxyl domain and assembly of procollagen I. J. Biol. Chem., 261, 8924-8935.
10. Gurevich, V.V., Pokrovskaya, I.D., Obukhova, T.A. and Zozulya, S.A. (1991) Preparative in vitro mRNA synthesis using SP6 and T7 polymerases. Anal. Biochem., 195, 207-213.
11. Hojima, Y., van der Rest, M. and Prockop, D.J. (1985) Type I procollagen carboxy-tenninal proteinase from chick embryo tendons. J. Biol. Chem., 260, 15996-16003.
12. Horton, R.M. (1993) PCR protocols: current methods and applications. In White, B.A. (ed.), Methods in Molecular Biology. Humana Press Inc., Totowa, NJ, Vol. 15, Chapter 25.
13. Jiminez, S.A., Bashey, R.I., Benditt, M. and Yanowski, R. (1977) Identification of α1(I) collagen trimer in embryonic chick tendons and calvaria. Biochem. Biophys. Res. Commun., 78, 1354-1361.
14. Kadler, K. (1994) Fibril forming collagens. In Sheterline, P. (ed.), Protein profiles: Extracellular matrix 1. Academic Press, London, UK.
15. Kessler, E., Kazuhiko, T., Biniaminov, L., Brusel, M. and Greenspan, D.S. (1996) Bone morphogenic protein-1: The type I procollagen proteinase. Science, 271, 360-362.
16. Kielty, C.M., Hopkinson, I. and Grant, M.E. (1993) The collagen family: structure, assembly and organization in the extracellular matrix. In Royce, P.M. and Steinmann, B. (eds), Connective Tissues and its Heritable Disorders: Molecular, Genetic and Medical Aspects. Wiley-Liss Inc, pp. 103-147.
17. Kunkel, T.A., Roberts, J.D. and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol., 154, 367-382.
18. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
19. 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.
20. Moro, L. and Smith, B.D. (1977) Identification of α1(I) collagen trimer and normal type I collagen in a polyoma virus induced mouse tumour. Arch. Biochem. Biophys., 182, 33-41.
21. Olsen, B.R., Hoffman, H.-P. and Prockop, D.J. (1976) Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage. Arch. Biochem. Biophys., 175, 341-350.
22. Prockop, D.J. and Kivirikko, K.I. (1995) Collagens: Molecular biology, diseases and potential for therapy. Annu. Rev. Biochem., 64, 403-434.
23. Prockop, D.J., Olsen, A., Kontusaari, S., Hyland, J., Ala-Kokko, L., Vasan, N.S., Barton, E., Buck, S., Harrison, K. and Brent, R.L. (1990) Mutations in human procollagen genes. Ann. N Y Acad. Sci., 580, 330-339.
24. Schofield, D.J., Uitto, J. and Prockop, D.J. (1974) Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells. Biochemistry, 13, 1801-1806.
25. Van der Rest, M. and Garrone, R., (1991) Collagen family of proteins. FASEB J., 5, 2814-2823.
26. Wilson, R., Oliver, J., Brookman, J.L., High, S. and Bulleid, N.J. (1995) Development of a semi-permeabilized cell system to study the translocation, folding, assembly and transport of secretory proteins. Biochem J., 307, 679-687.