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Volumn 44, Issue 46, 2005, Pages 15269-15279

Structure and assembly of the heterotrimeric and homotrimeric C-propeptides of type I collagen: Significance of the α2(I) chain

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; CONFORMATIONS; MOLECULAR STRUCTURE; MONOMERS; OLIGOMERS; POLYMERIZATION;

EID: 27944457587     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0508338     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 0022998819 scopus 로고
    • Folding of carboxyl domain and assembly of procollagen I
    • Doege, K. J., and Fessler, J. H. (1986) Folding of carboxyl domain and assembly of procollagen I, J. Biol. Chem. 261, 8924-8934.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8924-8934
    • Doege, K.J.1    Fessler, J.H.2
  • 2
    • 0022415488 scopus 로고
    • Supramolecular assemblies of mRNA direct the coordinated synthesis of type I procollagen chains
    • Veis, A., Leibovich, S. J., Evans, J., and Kirk, T. Z. (1985) Supramolecular assemblies of mRNA direct the coordinated synthesis of type I procollagen chains, Proc. Natl. Acad. Sci. U.S.A. 82, 3693-3697.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 3693-3697
    • Veis, A.1    Leibovich, S.J.2    Evans, J.3    Kirk, T.Z.4
  • 3
    • 0024550210 scopus 로고
    • The coordinate synthesis and cotranslational assembly of type I procollagen
    • Veis, A., and Kirk, T. Z. (1989) The coordinate synthesis and cotranslational assembly of type I procollagen, J. Biol. Chem. 264, 3884-3889.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3884-3889
    • Veis, A.1    Kirk, T.Z.2
  • 4
    • 0028810252 scopus 로고
    • Relationships between translation of pro α1(I) and pro α2(I) mRNAs during synthesis of the type I procollagen heterotrimer
    • Hu, G., Tylzanowski, P., Inoue, H., and Veis, A. (1995) Relationships between translation of pro α1(I) and pro α2(I) mRNAs during synthesis of the type I procollagen heterotrimer, J. Cell. Biochem. 59, 214-234.
    • (1995) J. Cell. Biochem. , vol.59 , pp. 214-234
    • Hu, G.1    Tylzanowski, P.2    Inoue, H.3    Veis, A.4
  • 5
    • 0029869463 scopus 로고    scopus 로고
    • Posttranscriptional aspects of the biosynthesis of type I collagen pro-alpha chains. The effects of posttranslational modifications on synthesis pauses during the elongation of the pro α1(I) chain
    • Gura, T., Hu, G., and Veis, A. (1996) Posttranscriptional aspects of the biosynthesis of type I collagen pro-alpha chains. The effects of posttranslational modifications on synthesis pauses during the elongation of the pro α1(I) chain, J. Cell. Biochem. 61, 194-215.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 194-215
    • Gura, T.1    Hu, G.2    Veis, A.3
  • 6
    • 0029834980 scopus 로고    scopus 로고
    • Triple helix formation of procollagen type I can occur at the rough endoplasmic membrane
    • Beck, K., Boswell, B. A., Ridgway, C. C., and Bachinger, H. P. (1996) Triple helix formation of procollagen type I can occur at the rough endoplasmic membrane, J. Biol. Chem. 271, 21566-21573.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21566-21573
    • Beck, K.1    Boswell, B.A.2    Ridgway, C.C.3    Bachinger, H.P.4
  • 7
    • 0024320170 scopus 로고
    • A frameshift mutation in results in a truncated non-functional carboxyl-terminal pro alpha 1(I) propeptide of type I collagen in osteogenesis imperfecta
    • Bateman, J. F., Lamande, S. R., Dahl, H. H., Chan, D., Mascara, T., and Cole, W. G. (1989) A frameshift mutation in results in a truncated non-functional carboxyl-terminal pro alpha 1(I) propeptide of type I collagen in osteogenesis imperfecta, J. Biol. Chem. 264, 10960-10964.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10960-10964
    • Bateman, J.F.1    Lamande, S.R.2    Dahl, H.H.3    Chan, D.4    Mascara, T.5    Cole, W.G.6
  • 8
    • 0027203904 scopus 로고
    • Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta
    • Chessler, S. D., Wallis, G. A., and Byers, P. H. (1993) Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta, J. Biol. Chem. 268, 18218-18215.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18218-118215
    • Chessler, S.D.1    Wallis, G.A.2    Byers, P.H.3
  • 9
    • 0027182875 scopus 로고
    • BiP binds type I procollagen alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
    • Chessler, S. D., and Byers, P. H. (1993) BiP binds type I procollagen alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta, J. Biol. Chem. 268, 18226-18233.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18226-18233
    • Chessler, S.D.1    Byers, P.H.2
  • 10
    • 0029836546 scopus 로고    scopus 로고
    • The phenotypic features of osteogenesis imperfecta resulting from a mutation of the carboxyl-terminal pro alpha 1(I) propeptide that impairs the assembly of type I procollagen and the extracellular matrix
    • Cole, W. G., Chow, C. W., Bateman, J. F., and Sillence, D. O. (1996) The phenotypic features of osteogenesis imperfecta resulting from a mutation of the carboxyl-terminal pro alpha 1(I) propeptide that impairs the assembly of type I procollagen and the extracellular matrix, J. Med. Genet. 33, 965-967.
    • (1996) J. Med. Genet. , vol.33 , pp. 965-967
    • Cole, W.G.1    Chow, C.W.2    Bateman, J.F.3    Sillence, D.O.4
  • 11
    • 0034937681 scopus 로고    scopus 로고
    • Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proalpha 1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfecta
    • Pace, J. M., Kuslich, C. D., Willing, M. C., and Byers, P. H. (2001) Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proalpha 1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfecta, J. Med. Genet. 38, 443-449.
    • (2001) J. Med. Genet. , vol.38 , pp. 443-449
    • Pace, J.M.1    Kuslich, C.D.2    Willing, M.C.3    Byers, P.H.4
  • 12
    • 0037485827 scopus 로고    scopus 로고
    • Changes in thermal stability and microunfolding pattern of collagen helix resulting from the loss of alpha2(I) chain in osteogenesis imperfecta murine
    • Kuznetsova, N. V., McBride, D. J., Jr., and Leikin, S. (2003) Changes in thermal stability and microunfolding pattern of collagen helix resulting from the loss of alpha2(I) chain in osteogenesis imperfecta murine, J. Mol. Biol. 33, 191-200.
    • (2003) J. Mol. Biol. , vol.33 , pp. 191-200
    • Kuznetsova, N.V.1    McBride Jr., D.J.2    Leikin, S.3
  • 13
    • 0033609136 scopus 로고    scopus 로고
    • Assembly of the type I procollagen molecule: Selectivity of the interactions between the pro-α1(I) and pro-α2(I)-carboxyl propeptides
    • Alvares, K., Siddiqui, F., Malone, J. P., and Veis, A. (1999) Assembly of the type I procollagen molecule: Selectivity of the interactions between the pro-α1(I) and pro-α2(I)-carboxyl propeptides, Biochemistry 38, 5401-5411.
    • (1999) Biochemistry , vol.38 , pp. 5401-5411
    • Alvares, K.1    Siddiqui, F.2    Malone, J.P.3    Veis, A.4
  • 14
    • 0023259571 scopus 로고
    • Disulfide bonding as a determinant of the molecular composition of types I, II, and III procollagen
    • Koivu, J. (1987) Disulfide bonding as a determinant of the molecular composition of types I, II, and III procollagen, FEBS Lett. 217, 216-220.
    • (1987) FEBS Lett. , vol.217 , pp. 216-220
    • Koivu, J.1
  • 16
    • 0037163051 scopus 로고    scopus 로고
    • Crystal structure of NC1 domains. Structuralbasis for type iv collagen assembly in basement membranes
    • Sundaramoorthy, M., Meiyappan, M., Todd, P., and Hudson, B. G. (2002) Crystal structure of NC1 domains. Structuralbasis for type iv collagen assembly in basement membranes, J. Biol. Chem. 277, 31142-31153.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31142-31153
    • Sundaramoorthy, M.1    Meiyappan, M.2    Todd, P.3    Hudson, B.G.4
  • 17
    • 0032536859 scopus 로고    scopus 로고
    • Crystal structure of the angiogenesis inhibitor endostatin at 1.5 Å resolution
    • Hohenester, E., Sasaki, T., Olsen, B. R., and Timpl, R. (1998) Crystal structure of the angiogenesis inhibitor endostatin at 1.5 Å resolution, EMBO J. 17, 1656-1664.
    • (1998) EMBO J. , vol.17 , pp. 1656-1664
    • Hohenester, E.1    Sasaki, T.2    Olsen, B.R.3    Timpl, R.4
  • 18
    • 0031916031 scopus 로고    scopus 로고
    • Molecular recognition in procollagen chain assembly
    • McLaughlin, S. H., and Bulleid, N. J. (1998) Molecular recognition in procollagen chain assembly, Matrix Biol. 16, 369-377.
    • (1998) Matrix Biol. , vol.16 , pp. 369-377
    • McLaughlin, S.H.1    Bulleid, N.J.2
  • 19
    • 0030812651 scopus 로고    scopus 로고
    • The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or triple helix folding
    • 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 triple helix folding, EMBO J. 16, 6694-6701.
    • (1997) EMBO J. , vol.16 , pp. 6694-6701
    • Bulleid, N.J.1    Dalley, J.A.2    Lees, J.F.3
  • 21
    • 0031595390 scopus 로고    scopus 로고
    • Role of the pro-alpha2(I) COOH-terminal region in assembly of type I collagen: Truncation of the last 10 amino acid residues of pro-alpha2(I) chain prevents assembly of type I collagen heterotrimer
    • Lim, A. L., Doyle, S. A., Balian, G., and Smith, B. D. (1998) Role of the pro-alpha2(I) COOH-terminal region in assembly of type I collagen: truncation of the last 10 amino acid residues of pro-alpha2(I) chain prevents assembly of type I collagen heterotrimer, J. Cell. Biochem. 71, 216-232.
    • (1998) J. Cell. Biochem. , vol.71 , pp. 216-232
    • Lim, A.L.1    Doyle, S.A.2    Balian, G.3    Smith, B.D.4
  • 22
    • 0031595391 scopus 로고    scopus 로고
    • Role of the pro-alpha2(I) COOH-terminal region in assembly of type I collagen: Disruption of two intramolecular disulfide bonds in pro-alpha2(I) blocks assembly of type I collagen
    • Doyle, S. A., and Smith, B. D. (1998) Role of the pro-alpha2(I) COOH-terminal region in assembly of type I collagen: disruption of two intramolecular disulfide bonds in pro-alpha2(I) blocks assembly of type I collagen, J. Cell. Biochem. 71, 233-242.
    • (1998) J. Cell. Biochem. , vol.71 , pp. 233-242
    • Doyle, S.A.1    Smith, B.D.2
  • 23
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • Hohenester, E., and Engel, J. (2002) Domain structure and organisation in extracellular matrix proteins, Matrix Biol. 21, 115-128.
    • (2002) Matrix Biol. , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 24
    • 0036447070 scopus 로고    scopus 로고
    • Building collagen molecules, fibrils, and suprafibrillar structures
    • Hulmes, D. J. (2002) Building collagen molecules, fibrils, and suprafibrillar structures, J. Struct. Biol. 137, 2-10.
    • (2002) J. Struct. Biol. , vol.137 , pp. 2-10
    • Hulmes, D.J.1
  • 25
    • 0034254089 scopus 로고    scopus 로고
    • What are oligomerization domains good for?
    • Engel, J., and Kammerer, R. A. (2000) What are oligomerization domains good for? Matrix Biol. 19, 283-288.
    • (2000) Matrix Biol. , vol.19 , pp. 283-288
    • Engel, J.1    Kammerer, R.A.2
  • 26
    • 0142211233 scopus 로고    scopus 로고
    • Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily
    • McAlinden, A., Smith, T. A., Sandell, L. J., Ficheux, D., Parry, D. A., and Hulmes, D. J. (2003) Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily, J. Biol. Chem. 278, 42200-42207.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42200-42207
    • McAlinden, A.1    Smith, T.A.2    Sandell, L.J.3    Ficheux, D.4    Parry, D.A.5    Hulmes, D.J.6
  • 27
    • 0033076317 scopus 로고    scopus 로고
    • Type I procollagen heterotrimer assembly is linked to subtle differences in the structures of the pro-α1(I) and pro-α2(I)-carboxyl propeptides
    • Veis, A., Alvares, K., and Malone, J. P. (1999) Type I procollagen heterotrimer assembly is linked to subtle differences in the structures of the pro-α1(I) and pro-α2(I)-carboxyl propeptides, Proc. Indian Acad. Sci. (Chem. Sci.) 111, 115-120.
    • (1999) Proc. Indian Acad. Sci. (Chem. Sci.) , vol.111 , pp. 115-120
    • Veis, A.1    Alvares, K.2    Malone, J.P.3
  • 28
    • 0035966016 scopus 로고    scopus 로고
    • Biophysical characterization of the C-propeptide trimer from human procollagen III reveals a tri-lobed structure
    • Bernocco, S., Finet, S., Ebel, C., Eichenberger, D., Mazzorana, M., Farjanel, J., and Hulmes, D. J. (2001) Biophysical characterization of the C-propeptide trimer from human procollagen III reveals a tri-lobed structure, J. Biol. Chem. 276, 48930-48936.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48930-48936
    • Bernocco, S.1    Finet, S.2    Ebel, C.3    Eichenberger, D.4    Mazzorana, M.5    Farjanel, J.6    Hulmes, D.J.7
  • 29
    • 0347089141 scopus 로고    scopus 로고
    • Type I collagen N-telopeptides adopt an ordered structure when docked to their helix receptor during fibrillogenesis
    • Malone, J. P., George, A., and Veis, A. (2004) Type I collagen N-telopeptides adopt an ordered structure when docked to their helix receptor during fibrillogenesis, Proteins: Struct., Funct., Bioinf. 54, 206-215.
    • (2004) Proteins: Struct., Funct., Bioinf. , vol.54 , pp. 206-215
    • Malone, J.P.1    George, A.2    Veis, A.3
  • 30
    • 10644276299 scopus 로고    scopus 로고
    • Heterotrimeric type I C-telopeptide conformation as docked to its helix receptor
    • Malone, J. P., and Veis, A. (2004) Heterotrimeric type I C-telopeptide conformation as docked to its helix receptor, Biochemistry 43, 15358-15366.
    • (2004) Biochemistry , vol.43 , pp. 15358-15366
    • Malone, J.P.1    Veis, A.2
  • 35
    • 0023131688 scopus 로고
    • Identification of disulfide bonds in carboxy-terminal propeptides of human type I procollagen
    • Koivu, J. (1987) Identification of disulfide bonds in carboxy-terminal propeptides of human type I procollagen, FEBS Lett. 212, 229-232.
    • (1987) FEBS Lett. , vol.212 , pp. 229-232
    • Koivu, J.1
  • 36
    • 0023644751 scopus 로고
    • Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation
    • Koivu, J., and Myllyla, R. (1987) Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation, J. Biol. Chem. 262, 6159-6164.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6159-6164
    • Koivu, J.1    Myllyla, R.2
  • 39
    • 0029021323 scopus 로고
    • The type I pro alpha 1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis
    • Lamande, S. R., and Bateman, J. F. (1995) The type I pro alpha 1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis, J. Biol. Chem. 270, 17858-17865.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17858-17865
    • Lamande, S.R.1    Bateman, J.F.2
  • 40
    • 0017739466 scopus 로고
    • Purification and characterization of a peptide from the carboxyl-terminal region of chick tendon procollagen type I
    • Olsen, B. R., Cuzman, N. A., Engel, J., Condit, C., and Aase, S. (1977) Purification and characterization of a peptide from the carboxyl-terminal region of chick tendon procollagen type I, Biochemistry 16, 3030-3036.
    • (1977) Biochemistry , vol.16 , pp. 3030-3036
    • Olsen, B.R.1    Cuzman, N.A.2    Engel, J.3    Condit, C.4    Aase, S.5
  • 41
    • 0030606256 scopus 로고    scopus 로고
    • Crystal structures and solution conformations of a dominant negative mutant of Escherichia coli maltose-binding protein
    • Shilton, B. H., Shuman, H. A., and Mowbray, S. L. (1996) Crystal structures and solution conformations of a dominant negative mutant of Escherichia coli maltose-binding protein, J. Mol. Biol. 264, 364-376.
    • (1996) J. Mol. Biol. , vol.264 , pp. 364-376
    • Shilton, B.H.1    Shuman, H.A.2    Mowbray, S.L.3
  • 42
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose- Or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G. Y., and Quiocho, F. A. (1991) The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis, J. Biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.Y.2    Quiocho, F.A.3
  • 43
    • 0002430286 scopus 로고
    • Organization and evolution of the fibrillar collagen genes
    • Olsen, B. R., and Nimni, M. E., Eds. CRC Press, Boca Raton, FL
    • Ramirez, F. (1989) Organization and evolution of the fibrillar collagen genes, in Collagen (Olsen, B. R., and Nimni, M. E., Eds.) Vol. 4, pp 21-30, CRC Press, Boca Raton, FL.
    • (1989) Collagen , vol.4 , pp. 21-30
    • Ramirez, F.1
  • 46
    • 0028031170 scopus 로고
    • Hsp47 and the translation-translocation machinery cooperate in the production of alpha 1(I) chains of type I procollagen
    • Sauk, J. J., Smith, T., Norris, K., and Ferreira, L. (1994) Hsp47 and the translation-translocation machinery cooperate in the production of alpha 1(I) chains of type I procollagen, J. Biol. Chem. 269, 3941-3946.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3941-3946
    • Sauk, J.J.1    Smith, T.2    Norris, K.3    Ferreira, L.4
  • 47
    • 0028656507 scopus 로고
    • Association of Hsp47, Grp78, and Grp94 with procollagen supports the successive or coupled action of molecular chaperones
    • Ferreira, L. R., Norris, K., Smith, T., Hebert, C., and Sauk, J. J. (1994) Association of Hsp47, Grp78, and Grp94 with procollagen supports the successive or coupled action of molecular chaperones, J. Cell. Biochem. 56, 518-526.
    • (1994) J. Cell. Biochem. , vol.56 , pp. 518-526
    • Ferreira, L.R.1    Norris, K.2    Smith, T.3    Hebert, C.4    Sauk, J.J.5
  • 48
    • 0007152183 scopus 로고
    • Procollagen segment-long-spacing crystallites: Their role in collagen fibrillogenesis
    • Bruns, R. R., Hulmes, D. J. S., Therrien, S. F., and Gross, J. (1979) Procollagen segment-long-spacing crystallites: Their role in collagen fibrillogenesis, Proc. Natl. Acad. Sci. U.S.A. 76, 313-317.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 313-317
    • Bruns, R.R.1    Hulmes, D.J.S.2    Therrien, S.F.3    Gross, J.4


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