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Volumn 16, Issue 22, 1997, Pages 6694-6701

The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis

Author keywords

Haemagglutinin transmembrane domain; Procollagen folding; Trimerization

Indexed keywords

HYDROXYPROLINE; MEMBRANE PROTEIN; PROCOLLAGEN;

EID: 0030812651     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.22.6694     Document Type: Article
Times cited : (88)

References (27)
  • 1
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen: Role of disultide bridges and peptide bond isomcrization
    • Bächinger,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 disultide bridges and peptide bond isomcrization. Eur. J. Biochem., 106, 619-632.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 619-632
    • Bächinger, H.-P.1    Bruckner, P.2    Timpl, R.3    Prockop, D.J.4    Engel, J.5
  • 2
    • 0019768629 scopus 로고
    • Chain assembly intermediate in the biosynthesis of type III procollagen in chick embryo blood vessels
    • 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.
    • (1981) J. Biol. Chem. , vol.256 , pp. 13193-13199
    • Bachinger, H.-P.1    Fessler, L.I.2    Timpl, R.3    Fessler, J.H.4
  • 3
    • 0015624009 scopus 로고
    • The thermal transition of a nonhydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilising the triple helix of collagen
    • Berg,R.A. and Prockop.D.J. (1973) The thermal transition of a nonhydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilising the triple helix of collagen. Biochem. Biophys. Res. Commun., 52, 115-120.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 4
    • 0019880195 scopus 로고
    • Proteolytic enzymes as probes for the triple-helical conformation of procollagen
    • Bruckner,P. and Prockop,D.J. (1981) Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal. Biochem., 110. 360-368.
    • (1981) Anal. Biochem. , vol.110 , pp. 360-368
    • Bruckner, P.1    Prockop, D.J.2
  • 5
    • 0018270937 scopus 로고
    • Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix to coil transition
    • Bruckner.P., Bachinger,H.-P., Timpl,R. and Engel,J. (1978) Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix to coil transition. Eur. J. Biockem., 90, 595-603.
    • (1978) Eur. J. Biockem. , vol.90 , pp. 595-603
    • Bruckner, P.1    Bachinger, H.-P.2    Timpl, R.3    Engel, J.4
  • 6
    • 0001157739 scopus 로고    scopus 로고
    • Novel approach to study the initial events in the folding and assembly of procollagen
    • Bulleid,N.J. (1996) Novel approach to study the initial events in the folding and assembly of procollagen. Semin. Cell Dev. Biol., 7. 667-672.
    • (1996) Semin. Cell Dev. Biol. , vol.7 , pp. 667-672
    • Bulleid, N.J.1
  • 7
    • 0029893377 scopus 로고    scopus 로고
    • 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
    • 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.
    • (1996) Biochem. J. , vol.317 , pp. 195-202
    • Bulleid, N.J.1    Wilson, R.2    Lees, J.F.3
  • 8
    • 0026648969 scopus 로고
    • Defective folding and stable association with protein disultide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the proα2(I) chain that preserves the Gly-X-Y repeat pattern
    • Chessler,S.D. and Byers,P.H. (1992) Defective folding and stable association with protein disultide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the proα2(I) chain that preserves the Gly-X-Y repeat pattern. J. Biol. Chem., 267, 7751-7757.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7751-7757
    • Chessler, S.D.1    Byers, P.H.2
  • 9
    • 0023142864 scopus 로고
    • COOH-terminal propeptides of the major human procollagens: Structural, functional and genetic comparisons
    • 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.
    • (1987) J. Mol. Biol. , vol.193 , pp. 127-143
    • Dion, A.S.1    Myers, J.C.2
  • 10
    • 0022998819 scopus 로고
    • Folding of carboxyl domain and assembly of procollagen I
    • Doege,KJ., and Fessler,J.H. (1986) Folding of carboxyl domain and assembly of procollagen I. J. Biol. Chem., 261, 8924-8935.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8924-8935
    • Doege, K.J.1    Fessler, J.H.2
  • 12
    • 0025904728 scopus 로고
    • The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
    • Engel,J. and Prockop,D.J. (1991) The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Anna. Rev. Biophys. Chem., 20. 137-152.
    • (1991) Anna. Rev. Biophys. Chem. , vol.20 , pp. 137-152
    • Engel, J.1    Prockop, D.J.2
  • 13
    • 0019828188 scopus 로고
    • Assembly and processing of procollagen type HI in chick embryo blood vessels
    • Fessler,L.I., Timpl,R. and Fessler,J.H. (1981) Assembly and processing of procollagen type HI in chick embryo blood vessels. J. Biol. Chem., 256, 2531-2537.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2531-2537
    • Fessler, L.I.1    Timpl, R.2    Fessler, J.H.3
  • 16
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • Harding,J.J. and Crabbe,M.J.C. (eds). CRC Press. Boca Raton, FL
    • 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,M.J.C. (eds). Post-translational Modification of Proteins. CRC Press. Boca Raton, FL, pp. 1-51.
    • (1992) Post-translational Modification of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 17
    • 0027967277 scopus 로고
    • The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen
    • 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.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24354-24360
    • Lees, J.F.1    Bulleid, N.J.2
  • 18
    • 0031055069 scopus 로고    scopus 로고
    • Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen
    • 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.
    • (1997) EMBO J. , vol.16 , pp. 908-916
    • Lees, J.-F.1    Tasab, M.2    Bulleid, N.J.3
  • 19
    • 0027516218 scopus 로고
    • Mechanisms of collagen trimer formation: Construction and expression of a recombinant minigene in HeLa cells reveals a direct effect of prolyl hydroxylation on chain assembly of type XII collagen
    • Mazzorana,M., Gruffat,H., Sergeant,A. and van der Rest,M. (1992) Mechanisms of collagen trimer formation: construction and expression of a recombinant minigene in HeLa cells reveals a direct effect of prolyl hydroxylation on chain assembly of type XII collagen. J. Biol. Chem., 268, 3029-3032.
    • (1992) J. Biol. Chem. , vol.268 , pp. 3029-3032
    • Mazzorana, M.1    Gruffat, H.2    Sergeant, A.3    Van der Rest, M.4
  • 20
    • 0029055303 scopus 로고
    • Trimeric assembly of collagen XII: Effect of deletion of the C-propeptide part of the molecule
    • Mazzorana,M., Giry-Lozinguez,C. and van der Rest,M. (1994) Trimeric assembly of collagen XII: effect of deletion of the C-propeptide part of the molecule. Matrix Biol., 14, 583-588.
    • (1994) Matrix Biol. , vol.14 , pp. 583-588
    • Mazzorana, M.1    Giry-Lozinguez, C.2    Van der Rest, M.3
  • 21
    • 0029800331 scopus 로고    scopus 로고
    • Involvement of prolyl 4-hydroxylase in the assembly of trimeric minicollagen XII: Study in a baculovirus expression system
    • Mazzorana,M., Snellman, Kivirikko,K.I., van der Rest,M. and Pihlajaniemi,T. (1996) Involvement of prolyl 4-hydroxylase in the assembly of trimeric minicollagen XII: study in a baculovirus expression system. J. Biol. Chem., 271, 29003-29008.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29003-29008
    • Mazzorana, M.1    Snellman2    Kivirikko, K.I.3    Van der Rest, M.4    Pihlajaniemi, T.5
  • 22
    • 0026772964 scopus 로고
    • Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
    • 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.
    • (1992) J. Cell Biol. , vol.117 , pp. 903-914
    • Nakai, A.1    Satoh, M.2    Hirayoshi, K.3    Nagata, K.4
  • 23
    • 0017183462 scopus 로고
    • Interchain disulfide bonds at the COOH-terminal end of procollagen synthesised by matrix-free cells from chick embryonic tendon and cartilage
    • Olsen,B-R., Hoffman,H.-P. and Prockop,D.J. (1976) Interchain disulfide bonds at the COOH-terminal end of procollagen synthesised by matrix-free cells from chick embryonic tendon and cartilage. Arch. Biochem. Biophys., 175, 341-350.
    • (1976) Arch. Biochem. Biophys. , vol.175 , pp. 341-350
    • Olsen, B.-R.1    Hoffman, H.-P.2    Prockop, D.J.3
  • 24
    • 0016248615 scopus 로고
    • Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells
    • 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.
    • (1974) Biochemistry , vol.13 , pp. 1801-1806
    • Schofield, D.J.1    Uitto, J.2    Prockop, D.J.3
  • 25
    • 0025037651 scopus 로고
    • Intracellular transport of soluble and membrane-bound glycoproteins: Folding, assembly and secretion of anchor-free influenza hemagglutinin
    • Singh, I., Doms,R.W., Wagner,K. and Helenius,A. (1990) Intracellular transport of soluble and membrane-bound glycoproteins: folding, assembly and secretion of anchor-free influenza hemagglutinin. EMBO J., 9, 631-639.
    • (1990) EMBO J. , vol.9 , pp. 631-639
    • Singh, I.1    Doms, R.W.2    Wagner, K.3    Helenius, A.4
  • 26
    • 0028906029 scopus 로고
    • Folding and oligomerizalion of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu,U., Hammond,C. and Helenius.A. (1995) Folding and oligomerizalion of influenza hemagglutinin in the ER and the intermediate compartment. EMBO J., 14, 1340-1348.
    • (1995) EMBO J. , vol.14 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 27
    • 0029024163 scopus 로고
    • Development of a semi-permcabilised cell system to study the translocation, folding, assembly and transport of secretory proteins
    • Wilson,R., Allen,A.J., Oliver,J., Brookman,J.L., High,S. and Bulleid,N.J. (1995) Development of a semi-permcabilised cell system to study the translocation, folding, assembly and transport of secretory proteins. Biochem J., 307, 679-687.
    • (1995) Biochem J. , vol.307 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6


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