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Volumn 19, Issue 4, 2010, Pages 775-785

Noncollagenous region of the streptococcal collagen-like protein is a trimerization domain that supports refolding of adjacent homologous and heterologous collagenous domains

Author keywords

Collagen; Folding; Streptococcus; Trimerization; Triple helix

Indexed keywords

BACTERIAL PROTEIN; BIOMATERIAL; COLLAGEN; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR TAL1;

EID: 77950259337     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.356     Document Type: Article
Times cited : (23)

References (44)
  • 1
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 a resolution
    • Bella J, Eaton M, Brodsky B, Berman HM (1994) Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science 266:75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 2
    • 0014381820 scopus 로고
    • Interchain hydrogen bonds via bound water molecules in the collagen triple helix
    • Ramachandran GN, Chandrasekharan R (1968) Interchain hydrogen bonds via bound water molecules in the collagen triple helix. Biopolymers 6:1649-1658.
    • (1968) Biopolymers , vol.6 , pp. 1649-1658
    • Ramachandran, G.N.1    Chandrasekharan, R.2
  • 3
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich A, Crick FH (1961)The molecular structure of collagen. J Mol Biol 3:483-506.
    • (1961) J Mol Biol , vol.3 , pp. 483-506
    • Rich, A.1    Crick, F.H.2
  • 4
    • 0042357053 scopus 로고    scopus 로고
    • Genome-based identification and analysis of collagen-related structural motifs in bacterial and viral proteins
    • Rasmussen M, Jacobsson M, Bjorck L (2003) Genome-based identification and analysis of collagen-related structural motifs in bacterial and viral proteins. J Biol Chem 278:32313-32316.
    • (2003) J Biol Chem , vol.278 , pp. 32313-32316
    • Rasmussen, M.1    Jacobsson, M.2    Bjorck, L.3
  • 5
    • 65249168279 scopus 로고    scopus 로고
    • Recombinant collagen trimers from insect cells and yeast
    • Myllyharju J (2009) Recombinant collagen trimers from insect cells and yeast. Methods Mol Biol 522:51-62.
    • (2009) Methods Mol Biol , vol.522 , pp. 51-62
    • Myllyharju, J.1
  • 6
    • 0037178812 scopus 로고    scopus 로고
    • Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices
    • Xu Y, Keene DR, Bujnicki JM, Hook M, Lukomski S (2002) Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices. J Biol Chem 277:27312-27318.
    • (2002) J Biol Chem , vol.277 , pp. 27312-27318
    • Xu, Y.1    Keene, D.R.2    Bujnicki, J.M.3    Hook, M.4    Lukomski, S.5
  • 7
    • 35648946905 scopus 로고    scopus 로고
    • Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline
    • Mohs A, Silva T, Yoshida T, Amin R, Lukomski S, Inouye M, Brodsky B (2007) Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline. J Biol Chem 282:29757-29765.
    • (2007) J Biol Chem , vol.282 , pp. 29757-29765
    • Mohs, A.1    Silva, T.2    Yoshida, T.3    Amin, R.4    Lukomski, S.5    Inouye, M.6    Brodsky, B.7
  • 8
    • 66349116433 scopus 로고    scopus 로고
    • Self-association of streptococcus pyogenes collagen-like constructs into higher order structures
    • Yoshizumi A, Yu Z, Silva T, Thiagarajan G, Ramshaw JA, Inouye M, Brodsky B (2009) Self-association of streptococcus pyogenes collagen-like constructs into higher order structures. Protein Sci 18:1241-1251.
    • (2009) Protein Sci , vol.18 , pp. 1241-1251
    • Yoshizumi, A.1    Yu, Z.2    Silva, T.3    Thiagarajan, G.4    Ramshaw, J.A.5    Inouye, M.6    Brodsky, B.7
  • 9
    • 22544432231 scopus 로고    scopus 로고
    • Orientation within the exosporium and structural stability of the collagen-like glycoprotein BclA of Bacillus anthracis
    • Boydston JA, Chen P, Steichen CT, Turnbough CL, Jr (2005) Orientation within the exosporium and structural stability of the collagen-like glycoprotein BclA of Bacillus anthracis. J Bacteriol 187:5310-5317.
    • (2005) J Bacteriol , vol.187 , pp. 5310-5317
    • Boydston, J.A.1    Chen, P.2    Steichen, C.T.3    Turnbough Jr., C.L.4
  • 10
    • 0037113093 scopus 로고    scopus 로고
    • New functional roles for noncollagenous domains of basement membrane collagens
    • Ortega N, Werb Z (2002) New functional roles for noncollagenous domains of basement membrane collagens. J Cell Sci 115:4201-4214.
    • (2002) J Cell Sci , vol.115 , pp. 4201-4214
    • Ortega, N.1    Werb, Z.2
  • 11
    • 0030297699 scopus 로고    scopus 로고
    • Domain organizations of modular extracellular matrix proteins and their evolution
    • Engel J (1996) Domain organizations of modular extracellular matrix proteins and their evolution. Matrix Biol 15:295-299.
    • (1996) Matrix Biol , vol.15 , pp. 295-299
    • Engel, J.1
  • 12
    • 33846029867 scopus 로고    scopus 로고
    • Molecular recognition in the assembly of collagens: Terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers
    • Khoshnoodi J, Cartailler JP, Alvares K, Veis A, Hudson BG (2006) Molecular recognition in the assembly of collagens: terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers. J Biol Chem 281:38117-38121.
    • (2006) J Biol Chem , vol.281 , pp. 38117-38121
    • Khoshnoodi, J.1    Cartailler, J.P.2    Alvares, K.3    Veis, A.4    Hudson, B.G.5
  • 14
    • 30044440000 scopus 로고    scopus 로고
    • The crystal structure of the Bacillus anthracis spore surface protein BclA shows remarkable similarity to mammalian proteins
    • Rety S, Salamitou S, Garcia-Verdugo I, Hulmes DJ, Le Hegarat F, Chaby R, Lewit-Bentley A (2005)The crystal structure of the Bacillus anthracis spore surface protein BclA shows remarkable similarity to mammalian proteins. J Biol Chem 280:43073-43078.
    • (2005) J Biol Chem , vol.280 , pp. 43073-43078
    • Rety, S.1    Salamitou, S.2    Garcia-Verdugo, I.3    Hulmes, D.J.4    Le Hegarat, F.5    Chaby, R.6    Lewit-Bentley, A.7
  • 15
    • 77749279774 scopus 로고    scopus 로고
    • Sequence motifs and proteolytic cleavage of the collagen-like glycoprotein BclA required for its attachment to the exosporium of Bacillus anthracis
    • Tan L, Turnbough CL, Jr (2010) Sequence motifs and proteolytic cleavage of the collagen-like glycoprotein BclA required for its attachment to the exosporium of Bacillus anthracis. J Bacteriol 192(5):1259-1268
    • (2010) J Bacteriol , vol.192 , Issue.5 , pp. 1259-1268
    • Tan, L.1    Turnbough Jr., C.L.2
  • 16
    • 0034441340 scopus 로고    scopus 로고
    • Identification and characterization of the scl gene encoding a group a Streptococcus extracellular protein virulence factor with similarity to human collagen
    • Lukomski S, Nakashima K, Abdi I, Cipriano VJ, Ireland RM, Reid SD, Adams GG, Musser JM (2000) Identification and characterization of the scl gene encoding a group A Streptococcus extracellular protein virulence factor with similarity to human collagen. Infect Immun 68:6542-6553.
    • (2000) Infect Immun , vol.68 , pp. 6542-6553
    • Lukomski, S.1    Nakashima, K.2    Abdi, I.3    Cipriano, V.J.4    Ireland, R.M.5    Reid, S.D.6    Adams, G.G.7    Musser, J.M.8
  • 17
    • 0033793665 scopus 로고    scopus 로고
    • SclA, a novel collagen-like surface protein of Streptococcus pyogenes
    • Rasmussen M, Eden A, Bjorck L (2000) SclA, a novel collagen-like surface protein of Streptococcus pyogenes. Infect Immun 68:6370-6377.
    • (2000) Infect Immun , vol.68 , pp. 6370-6377
    • Rasmussen, M.1    Eden, A.2    Bjorck, L.3
  • 18
    • 0035119161 scopus 로고    scopus 로고
    • Identification and characterization of a second extracellular collagen-like protein made by group a Streptococcus: Control of production at the level of translation
    • Lukomski S, Nakashima K, Abdi I, Cipriano VJ, Shelvin BJ, Graviss EA, Musser JM (2001)Identification and characterization of a second extracellular collagen-like protein made by group A Streptococcus: control of production at the level of translation. Infect Immun 69:1729-1738.
    • (2001) Infect Immun , vol.69 , pp. 1729-1738
    • Lukomski, S.1    Nakashima, K.2    Abdi, I.3    Cipriano, V.J.4    Shelvin, B.J.5    Graviss, E.A.6    Musser, J.M.7
  • 19
    • 0034938817 scopus 로고    scopus 로고
    • Unique regulation of SclB - A novel collagen-like surface protein of Streptococcus pyogenes
    • Rasmussen M, Bjorck L (2001) Unique regulation of SclB - a novel collagen-like surface protein of Streptococcus pyogenes. Mol Microbiol 40:1427-1438.
    • (2001) Mol Microbiol , vol.40 , pp. 1427-1438
    • Rasmussen, M.1    Bjorck, L.2
  • 20
    • 0035135740 scopus 로고    scopus 로고
    • Streptococcus pyogenes sclB encodes a putative hypervariable surface protein with a collagen-like repetitive structure
    • Whatmore AM (2001) Streptococcus pyogenes sclB encodes a putative hypervariable surface protein with a collagen-like repetitive structure. Microbiology 147:419-429.
    • (2001) Microbiology , vol.147 , pp. 419-429
    • Whatmore, A.M.1
  • 21
    • 17144397160 scopus 로고    scopus 로고
    • A streptococcal collagen-like protein interacts with the alpha2beta1 integrin and induces intracellular signaling
    • Humtsoe JO, Kim JK, Xu Y, Keene DR, Hook M, Lukomski S, Wary KK (2005) A streptococcal collagen-like protein interacts with the alpha2beta1 integrin and induces intracellular signaling. J Biol Chem 280:13848-13857.
    • (2005) J Biol Chem , vol.280 , pp. 13848-13857
    • Humtsoe, J.O.1    Kim, J.K.2    Xu, Y.3    Keene, D.R.4    Hook, M.5    Lukomski, S.6    Wary, K.K.7
  • 22
    • 34249808541 scopus 로고    scopus 로고
    • Scl1-dependent internalization of group a Streptococcus via direct interactions with the alpha2-beta(1) integrin enhances pathogen survival and reemergence
    • Caswell CC, Lukomska E, Seo NS, Hook M, Lukomski S (2007) Scl1-dependent internalization of group A Streptococcus via direct interactions with the alpha2-beta(1) integrin enhances pathogen survival and reemergence. Mol Microbiol 64:1319-1331.
    • (2007) Mol Microbiol , vol.64 , pp. 1319-1331
    • Caswell, C.C.1    Lukomska, E.2    Seo, N.S.3    Hook, M.4    Lukomski, S.5
  • 23
    • 74349093820 scopus 로고    scopus 로고
    • Scl1, the multifunctional adhesin of group a Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells
    • in press
    • Caswell CC, Oliver-Kozup H, Han R, Lukomska E, Lukomski S (in press) Scl1, the multifunctional adhesin of group A Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells. FEMS Microbiol Lett.
    • FEMS Microbiol Lett.
    • Caswell, C.C.1    Oliver-Kozup, H.2    Han, R.3    Lukomska, E.4    Lukomski, S.5
  • 24
    • 61349095442 scopus 로고    scopus 로고
    • Identification of the first prokaryotic collagen sequence motif that mediates binding to human collagen receptors, integrins alpha2-beta1 and alpha11beta1
    • Caswell CC, Barczyk M, Keene DR, Lukomska E, Gullberg DE, Lukomski S (2008) Identification of the first prokaryotic collagen sequence motif that mediates binding to human collagen receptors, integrins alpha2-beta1 and alpha11beta1. J Biol Chem 283:36168-36175.
    • (2008) J Biol Chem , vol.283 , pp. 36168-36175
    • Caswell, C.C.1    Barczyk, M.2    Keene, D.R.3    Lukomska, E.4    Gullberg, D.E.5    Lukomski, S.6
  • 25
    • 34548307247 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins a and B
    • Pahlman LI, Marx PF, Morgelin M, Lukomski S, Meijers JC, Herwald H (2007) Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins A and B. J Biol Chem 282:24873-24881.
    • (2007) J Biol Chem , vol.282 , pp. 24873-24881
    • Pahlman, L.I.1    Marx, P.F.2    Morgelin, M.3    Lukomski, S.4    Meijers, J.C.5    Herwald, H.6
  • 27
    • 76249130327 scopus 로고    scopus 로고
    • Expanding the family of collagen proteins: Recombinant bacterial collagens of varying composition form triple-helices of similar stability
    • Xu C, Yu Z, Inouye M, Brodsky B, Mirochnitchenko O (2010) Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability. Biomacromolecules 11(2):348-356
    • (2010) Biomacromolecules , vol.11 , Issue.2 , pp. 348-356
    • Xu, C.1    Yu, Z.2    Inouye, M.3    Brodsky, B.4    Mirochnitchenko, O.5
  • 28
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization
    • Bachinger HP, Bruckner P, Timpl R, Prockop DJ, Engel J (1980) Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur J Biochem 106:619-632.
    • (1980) Eur J Biochem , vol.106 , pp. 619-632
    • Bachinger, H.P.1    Bruckner, P.2    Timpl, R.3    Prockop, D.J.4    Engel, J.5
  • 29
    • 0028175514 scopus 로고
    • A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation
    • Hoppe HJ, Barlow PN, Reid KB (1994) A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation. FEBS Lett 344:191-195.
    • (1994) FEBS Lett , vol.344 , pp. 191-195
    • Hoppe, H.J.1    Barlow, P.N.2    Reid, K.B.3
  • 30
    • 0141621157 scopus 로고    scopus 로고
    • Type XIII collagen and some other transmembrane collagens contain two separate coiled-coil motifs, which may function as independent oligomerization domains
    • Latvanlehto A, Snellman A, Tu H, Pihlajaniemi T (2003) Type XIII collagen and some other transmembrane collagens contain two separate coiled-coil motifs, which may function as independent oligomerization domains. J Biol Chem 278:37590-37599.
    • (2003) J Biol Chem , vol.278 , pp. 37590-37599
    • Latvanlehto, A.1    Snellman, A.2    Tu, H.3    Pihlajaniemi, T.4
  • 31
    • 0142211233 scopus 로고    scopus 로고
    • Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily
    • Mcalinden A, Smith TA, Sandell LJ, Ficheux D, Parry DA, Hulmes DJ (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
  • 32
    • 0037163051 scopus 로고    scopus 로고
    • Crystal structure of NC1 domains. Structural basis for type IV collagen assembly in basement membranes
    • Sundaramoorthy M, Meiyappan M, Todd P, Hudson BG (2002) Crystal structure of NC1 domains. Structural basis 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
  • 33
    • 18344390410 scopus 로고    scopus 로고
    • The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link
    • Than ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W (2002) The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proc Natl Acad Sci USA 99:6607-6612.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6607-6612
    • Than, M.E.1    Henrich, S.2    Huber, R.3    Ries, A.4    Mann, K.5    Kuhn, K.6    Timpl, R.7    Bourenkov, G.P.8    Bartunik, H.D.9    Bode, W.10
  • 34
    • 0036175281 scopus 로고    scopus 로고
    • Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer
    • Bogin O, Kvansakul M, Rom E, Singer J, Yayon A, Hohenester E (2002) Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer. Structure 10:165-173.
    • (2002) Structure , vol.10 , pp. 165-173
    • Bogin, O.1    Kvansakul, M.2    Rom, E.3    Singer, J.4    Yayon, A.5    Hohenester, E.6
  • 35
    • 0038024555 scopus 로고    scopus 로고
    • Crystal structure of the collagen alpha1(VIII) NC1 trimer
    • Kvansakul M, Bogin O, Hohenester E, Yayon A (2003) Crystal structure of the collagen alpha1(VIII) NC1 trimer. Matrix Biol 22:145-152.
    • (2003) Matrix Biol , vol.22 , pp. 145-152
    • Kvansakul, M.1    Bogin, O.2    Hohenester, E.3    Yayon, A.4
  • 36
    • 69549130585 scopus 로고    scopus 로고
    • Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold
    • Boudko SP, Sasaki T, Engel J, Lerch TF, Nix J, Chapman MS, Bachinger HP (2009) Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold. J Mol Biol 392:787-802.
    • (2009) J Mol Biol , vol.392 , pp. 787-802
    • Boudko, S.P.1    Sasaki, T.2    Engel, J.3    Lerch, T.F.4    Nix, J.5    Chapman, M.S.6    Bachinger, H.P.7
  • 39
    • 0025904728 scopus 로고
    • The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
    • Engel J, Prockop DJ (1991) The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Annu Rev Biophys Biophys Chem 20:137-152.
    • (1991) Annu Rev Biophys Biophys Chem , vol.20 , pp. 137-152
    • Engel, J.1    Prockop, D.J.2
  • 40
    • 0013937468 scopus 로고
    • The renaturation of soluble collagen. Products formed at different temperatures
    • Beier G, Engel J (1966) The renaturation of soluble collagen. Products formed at different temperatures. Biochemistry 5:2744-2755.
    • (1966) Biochemistry , vol.5 , pp. 2744-2755
    • Beier, G.1    Engel, J.2
  • 42
    • 0042856841 scopus 로고    scopus 로고
    • Assembly of stable human type I and III collagen molecules from hydroxylated recombinant chains in the yeast Pichia pastoris. Effect of an engineered C-terminal oligomerization domain foldon
    • Pakkanen O, Hamalainen ER, Kivirikko KI, Myllyharju J (2003) Assembly of stable human type I and III collagen molecules from hydroxylated recombinant chains in the yeast Pichia pastoris. Effect of an engineered C-terminal oligomerization domain foldon. J Biol Chem 278:32478-32483.
    • (2003) J Biol Chem , vol.278 , pp. 32478-32483
    • Pakkanen, O.1    Hamalainen, E.R.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 43
    • 0037175005 scopus 로고    scopus 로고
    • Trimerization of the amino propeptide of type IIA procollagen using a 14-amino acid sequence derived from the coiled-coil neck domain of surfactant protein D
    • Mcalinden A, Crouch EC, Bann JG, Zhang P, Sandell LJ (2002) Trimerization of the amino propeptide of type IIA procollagen using a 14-amino acid sequence derived from the coiled-coil neck domain of surfactant protein D. J Biol Chem 277:41274-41281.
    • (2002) J Biol Chem , vol.277 , pp. 41274-41281
    • Mcalinden, A.1    Crouch, E.C.2    Bann, J.G.3    Zhang, P.4    Sandell, L.J.5
  • 44
    • 0031055069 scopus 로고    scopus 로고
    • Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen
    • Lees JF, Tasab M, Bulleid NJ (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


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