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Volumn 405, Issue 1, 2011, Pages 143-157

Synergy, structure and conformational flexibility of hybrid cellulosomes displaying various inter-cohesins linkers

Author keywords

celllulosome; cellulose; inter cohesins linker; intrinsically disordered protein

Indexed keywords

CELLULOSOME; COHESIN; HYBRID PROTEIN; PHOSPHORIC ACID; SCAFFOLD PROTEIN;

EID: 78650417465     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.10.013     Document Type: Article
Times cited : (34)

References (44)
  • 1
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer E.A., Belaich J.P., Shoham Y., and Lamed R. The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides Annu. Rev. Microbiol. 58 2004 521 554
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.P.2    Shoham, Y.3    Lamed, R.4
  • 3
    • 33947256880 scopus 로고    scopus 로고
    • Cellulosomes: Microbial nanomachines that display plasticity in quaternary structure
    • Gilbert H.J. Cellulosomes: microbial nanomachines that display plasticity in quaternary structure Mol. Microbiol. 63 2007 1568 1576
    • (2007) Mol. Microbiol. , vol.63 , pp. 1568-1576
    • Gilbert, H.J.1
  • 4
    • 69949130305 scopus 로고    scopus 로고
    • Diversity and strain specificity of plant cell wall degrading enzymes revealed by the draft genome of Ruminococcus flavefaciens FD-1
    • Berg Miller M.E., Antonopoulos D.A., Rincon M.T., Band M., Bari A., and Akraiko T. Diversity and strain specificity of plant cell wall degrading enzymes revealed by the draft genome of Ruminococcus flavefaciens FD-1 PLoS One 4 2009 e6650
    • (2009) PLoS One , vol.4 , pp. 6650
    • Berg Miller, M.E.1    Antonopoulos, D.A.2    Rincon, M.T.3    Band, M.4    Bari, A.5    Akraiko, T.6
  • 5
    • 47349130717 scopus 로고    scopus 로고
    • Cellulosome gene cluster analysis for gauging the diversity of the ruminal cellulolytic bacterium Ruminococcus flavefaciens
    • Jindou S., Brulc J.M., Levy-Assaraf M., Rincon M.T., Flint H.J., and Berg M.E. Cellulosome gene cluster analysis for gauging the diversity of the ruminal cellulolytic bacterium Ruminococcus flavefaciens FEMS Microbiol. Lett. 285 2008 188 194
    • (2008) FEMS Microbiol. Lett. , vol.285 , pp. 188-194
    • Jindou, S.1    Brulc, J.M.2    Levy-Assaraf, M.3    Rincon, M.T.4    Flint, H.J.5    Berg, M.E.6
  • 6
    • 27744600973 scopus 로고    scopus 로고
    • Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface
    • Rincon M.T., Cepeljnik T., Martin J.C., Lamed R., Barak Y., Bayer E.A., and Flint H.J. Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface J. Bacteriol. 187 2005 7569 7578
    • (2005) J. Bacteriol. , vol.187 , pp. 7569-7578
    • Rincon, M.T.1    Cepeljnik, T.2    Martin, J.C.3    Lamed, R.4    Barak, Y.5    Bayer, E.A.6    Flint, H.J.7
  • 7
    • 76649097005 scopus 로고    scopus 로고
    • Modulation of cellulosome composition in Clostridium cellulolyticum: Adaptation to the polysaccharide environment revealed by proteomic and carbohydrate-active enzyme analyses
    • Blouzard J.C., Coutinho P.M., Fierobe H.P., Henrissat B., Lignon S., and Tardif C. Modulation of cellulosome composition in Clostridium cellulolyticum: adaptation to the polysaccharide environment revealed by proteomic and carbohydrate-active enzyme analyses Proteomics 10 2010 541 554
    • (2010) Proteomics , vol.10 , pp. 541-554
    • Blouzard, J.C.1    Coutinho, P.M.2    Fierobe, H.P.3    Henrissat, B.4    Lignon, S.5    Tardif, C.6
  • 8
    • 0345628619 scopus 로고    scopus 로고
    • Sequence analysis of scaffolding protein CipC and ORFXp, a new cohesin-containing protein in Clostridium cellulolyticum: Comparison of various cohesin domains and subcellular localization of ORFXp
    • Pages S., Belaich A., Fierobe H.P., Tardif C., Gaudin C., and Belaich J.P. Sequence analysis of scaffolding protein CipC and ORFXp, a new cohesin-containing protein in Clostridium cellulolyticum: comparison of various cohesin domains and subcellular localization of ORFXp J. Bacteriol. 181 1999 1801 1810
    • (1999) J. Bacteriol. , vol.181 , pp. 1801-1810
    • Pages, S.1    Belaich, A.2    Fierobe, H.P.3    Tardif, C.4    Gaudin, C.5    Belaich, J.P.6
  • 9
    • 33947152858 scopus 로고    scopus 로고
    • Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: Identification of seven genes encoding new dockerin-containing proteins
    • Blouzard J.C., Bourgeois C., de Philip P., Valette O., Belaich A., and Tardif C. Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: identification of seven genes encoding new dockerin-containing proteins J. Bacteriol. 189 2007 2300 2309
    • (2007) J. Bacteriol. , vol.189 , pp. 2300-2309
    • Blouzard, J.C.1    Bourgeois, C.2    De Philip, P.3    Valette, O.4    Belaich, A.5    Tardif, C.6
  • 10
    • 0035877619 scopus 로고    scopus 로고
    • Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes
    • Fierobe H.P., Mechaly A., Tardif C., Belaich A., Lamed R., and Shoham Y. Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes J. Biol. Chem. 276 2001 21257 21261
    • (2001) J. Biol. Chem. , vol.276 , pp. 21257-21261
    • Fierobe, H.P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6
  • 11
    • 0343229549 scopus 로고    scopus 로고
    • Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain
    • Pages S., Belaich A., Belaich J.P., Morag E., Lamed R., Shoham Y., and Bayer E.A. Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain Proteins: Struct. Funct. Bioinformatics 29 1997 517 527
    • (1997) Proteins: Struct. Funct. Bioinformatics , vol.29 , pp. 517-527
    • Pages, S.1    Belaich, A.2    Belaich, J.P.3    Morag, E.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 12
    • 20944438012 scopus 로고    scopus 로고
    • Action of designer cellulosomes on homogeneous versus complex substrates: Controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin
    • Fierobe H.P., Mingardon F., Mechaly A., Belaich A., Rincon M.T., and Pages S. Action of designer cellulosomes on homogeneous versus complex substrates: controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin J. Biol. Chem. 280 2005 16325 16334
    • (2005) J. Biol. Chem. , vol.280 , pp. 16325-16334
    • Fierobe, H.P.1    Mingardon, F.2    Mechaly, A.3    Belaich, A.4    Rincon, M.T.5    Pages, S.6
  • 13
    • 0347579849 scopus 로고    scopus 로고
    • Degradation of cellulose substrates by cellulosome chimeras. Substrate targeting versus proximity of enzyme components
    • Fierobe H.P., Bayer E.A., Tardif C., Czjzek M., Mechaly A., and Belaich A. Degradation of cellulose substrates by cellulosome chimeras. Substrate targeting versus proximity of enzyme components J. Biol. Chem. 277 2002 49621 49630
    • (2002) J. Biol. Chem. , vol.277 , pp. 49621-49630
    • Fierobe, H.P.1    Bayer, E.A.2    Tardif, C.3    Czjzek, M.4    Mechaly, A.5    Belaich, A.6
  • 14
    • 0027285934 scopus 로고
    • Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL-protein reveals an unusual degree of internal homology
    • Gerngross U.T., Romaniec M.P., Kobayashi T., Huskisson N.S., and Demain A.L. Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL-protein reveals an unusual degree of internal homology Mol. Microbiol. 8 1993 325 334
    • (1993) Mol. Microbiol. , vol.8 , pp. 325-334
    • Gerngross, U.T.1    Romaniec, M.P.2    Kobayashi, T.3    Huskisson, N.S.4    Demain, A.L.5
  • 15
    • 11244296147 scopus 로고    scopus 로고
    • Structural insights into the mechanism of formation of cellulosomes probed by small angle X-ray scattering
    • Hammel M., Fierobe H.P., Czjzek M., Finet S., and Receveur-Brechot V. Structural insights into the mechanism of formation of cellulosomes probed by small angle X-ray scattering J. Biol. Chem. 279 2004 55985 55994
    • (2004) J. Biol. Chem. , vol.279 , pp. 55985-55994
    • Hammel, M.1    Fierobe, H.P.2    Czjzek, M.3    Finet, S.4    Receveur-Brechot, V.5
  • 16
    • 33644676351 scopus 로고    scopus 로고
    • Structural basis of cellulosome efficiency explored by small angle X-ray scattering
    • Hammel M., Fierobe H.P., Czjzek M., Kurkal V., Smith J.C., and Bayer E.A. Structural basis of cellulosome efficiency explored by small angle X-ray scattering J. Biol. Chem. 280 2005 38562 38568
    • (2005) J. Biol. Chem. , vol.280 , pp. 38562-38568
    • Hammel, M.1    Fierobe, H.P.2    Czjzek, M.3    Kurkal, V.4    Smith, J.C.5    Bayer, E.A.6
  • 17
    • 0030014350 scopus 로고    scopus 로고
    • Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to Trichoderma reesei cellobiohydrolase II
    • Denman S., Xue G.P., and Patel B. Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to Trichoderma reesei cellobiohydrolase II Appl. Environ. Microbiol. 62 1996 1889 1896
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1889-1896
    • Denman, S.1    Xue, G.P.2    Patel, B.3
  • 19
    • 69949099255 scopus 로고    scopus 로고
    • Processive endoglucanases mediate degradation of cellulose by Saccharophagus degradans
    • Watson B.J., Zhang H., Longmire A.G., Moon Y.H., and Hutcheson S.W. Processive endoglucanases mediate degradation of cellulose by Saccharophagus degradans J. Bacteriol. 191 2009 5697 5705
    • (2009) J. Bacteriol. , vol.191 , pp. 5697-5705
    • Watson, B.J.1    Zhang, H.2    Longmire, A.G.3    Moon, Y.H.4    Hutcheson, S.W.5
  • 20
    • 0026529913 scopus 로고
    • Primary sequence analysis of Clostridium cellulovorans cellulose binding protein A
    • Shoseyov O., Takagi M., Goldstein M.A., and Doi R.H. Primary sequence analysis of Clostridium cellulovorans cellulose binding protein A Proc. Natl Acad. Sci. USA 89 1992 3483 3487
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3483-3487
    • Shoseyov, O.1    Takagi, M.2    Goldstein, M.A.3    Doi, R.H.4
  • 21
    • 0030001273 scopus 로고    scopus 로고
    • A new type of cohesin domain that specifically binds the dockerin domain of the Clostridium thermocellum cellulosome-integrating protein CipA
    • Leibovitz E., and Beguin P. A new type of cohesin domain that specifically binds the dockerin domain of the Clostridium thermocellum cellulosome-integrating protein CipA J. Bacteriol. 178 1996 3077 3084
    • (1996) J. Bacteriol. , vol.178 , pp. 3077-3084
    • Leibovitz, E.1    Beguin, P.2
  • 22
    • 0030976037 scopus 로고    scopus 로고
    • Characterization and subcellular localization of the Clostridium thermocellum scaffoldin dockerin binding protein SdbA
    • Leibovitz E., Ohayon H., Gounon P., and Beguin P. Characterization and subcellular localization of the Clostridium thermocellum scaffoldin dockerin binding protein SdbA J. Bacteriol. 179 1997 2519 2523
    • (1997) J. Bacteriol. , vol.179 , pp. 2519-2523
    • Leibovitz, E.1    Ohayon, H.2    Gounon, P.3    Beguin, P.4
  • 23
    • 1142298547 scopus 로고    scopus 로고
    • Architecture of the Bacteroides cellulosolvens cellulosome: Description of a cell surface-anchoring scaffoldin and a family 48 cellulase
    • Xu Q., Bayer E.A., Goldman M., Kenig R., Shoham Y., and Lamed R. Architecture of the Bacteroides cellulosolvens cellulosome: description of a cell surface-anchoring scaffoldin and a family 48 cellulase J. Bacteriol. 186 2004 968 977
    • (2004) J. Bacteriol. , vol.186 , pp. 968-977
    • Xu, Q.1    Bayer, E.A.2    Goldman, M.3    Kenig, R.4    Shoham, Y.5    Lamed, R.6
  • 24
    • 0033901462 scopus 로고    scopus 로고
    • A scaffoldin of the Bacteroides cellulosolvens cellulosome that contains 11 type II cohesins
    • Ding S.Y., Bayer E.A., Steiner D., Shoham Y., and Lamed R. A scaffoldin of the Bacteroides cellulosolvens cellulosome that contains 11 type II cohesins J. Bacteriol. 182 2000 4915 4925
    • (2000) J. Bacteriol. , vol.182 , pp. 4915-4925
    • Ding, S.Y.1    Bayer, E.A.2    Steiner, D.3    Shoham, Y.4    Lamed, R.5
  • 25
    • 0032754343 scopus 로고    scopus 로고
    • A novel cellulosomal scaffoldin from Acetivibrio cellulolyticus that contains a family 9 glycosyl hydrolase
    • Ding S.Y., Bayer E.A., Steiner D., Shoham Y., and Lamed R. A novel cellulosomal scaffoldin from Acetivibrio cellulolyticus that contains a family 9 glycosyl hydrolase J. Bacteriol. 181 1999 6720 6729
    • (1999) J. Bacteriol. , vol.181 , pp. 6720-6729
    • Ding, S.Y.1    Bayer, E.A.2    Steiner, D.3    Shoham, Y.4    Lamed, R.5
  • 26
    • 0034711446 scopus 로고    scopus 로고
    • Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum
    • Mosbah A., Belaich A., Bornet O., Belaich J.P., Henrissat B., and Darbon H. Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum J. Mol. Biol. 304 2000 201 217
    • (2000) J. Mol. Biol. , vol.304 , pp. 201-217
    • Mosbah, A.1    Belaich, A.2    Bornet, O.3    Belaich, J.P.4    Henrissat, B.5    Darbon, H.6
  • 27
    • 0031857381 scopus 로고    scopus 로고
    • Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome
    • Kakiuchi M., Isui A., Suzuki K., Fujino T., Fujino E., and Kimura T. Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome J. Bacteriol. 180 1998 4303 4308
    • (1998) J. Bacteriol. , vol.180 , pp. 4303-4308
    • Kakiuchi, M.1    Isui, A.2    Suzuki, K.3    Fujino, T.4    Fujino, E.5    Kimura, T.6
  • 28
    • 0038443570 scopus 로고    scopus 로고
    • The cellulosome system of Acetivibrio cellulolyticus includes a novel type of adaptor protein and a cell surface anchoring protein
    • Xu Q., Gao W., Ding S.Y., Kenig R., Shoham Y., Bayer E.A., and Lamed R. The cellulosome system of Acetivibrio cellulolyticus includes a novel type of adaptor protein and a cell surface anchoring protein J. Bacteriol. 185 2003 4548 4557
    • (2003) J. Bacteriol. , vol.185 , pp. 4548-4557
    • Xu, Q.1    Gao, W.2    Ding, S.Y.3    Kenig, R.4    Shoham, Y.5    Bayer, E.A.6    Lamed, R.7
  • 32
    • 0027321971 scopus 로고
    • Adhesion and growth rate of Clostridium cellulolyticum ATCC 35319 on crystalline cellulose
    • Gelhaye E., Petitdemange H., and Gay R. Adhesion and growth rate of Clostridium cellulolyticum ATCC 35319 on crystalline cellulose J. Bacteriol. 175 1993 3452 3458
    • (1993) J. Bacteriol. , vol.175 , pp. 3452-3458
    • Gelhaye, E.1    Petitdemange, H.2    Gay, R.3
  • 34
    • 0027772063 scopus 로고
    • The nature of the carbohydrate-peptide linkage region in glycoproteins from the cellulosomes of Clostridium thermocellum and Bacteroides cellulosolvens
    • Gerwig G.J., Kamerling J.P., Vliegenthart J.F., Morag E., Lamed R., and Bayer E.A. The nature of the carbohydrate-peptide linkage region in glycoproteins from the cellulosomes of Clostridium thermocellum and Bacteroides cellulosolvens J. Biol. Chem. 268 1993 26956 26960
    • (1993) J. Biol. Chem. , vol.268 , pp. 26956-26960
    • Gerwig, G.J.1    Kamerling, J.P.2    Vliegenthart, J.F.3    Morag, E.4    Lamed, R.5    Bayer, E.A.6
  • 35
    • 0030700658 scopus 로고    scopus 로고
    • CelG from Clostridium cellulolyticum: A multidomain endoglucanase acting efficiently on crystalline cellulose
    • Gal L., Gaudin C., Belaich A., Pages S., Tardif C., and Belaich J.P. CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose J. Bacteriol. 179 1997 6595 6601
    • (1997) J. Bacteriol. , vol.179 , pp. 6595-6601
    • Gal, L.1    Gaudin, C.2    Belaich, A.3    Pages, S.4    Tardif, C.5    Belaich, J.P.6
  • 36
    • 0033613077 scopus 로고    scopus 로고
    • Cellulosome from Clostridium cellulolyticum: Molecular study of the dockerin/cohesin interaction
    • Fierobe H.P., Pages S., Belaich A., Champ S., Lexa D., and Belaich J.P. Cellulosome from Clostridium cellulolyticum: molecular study of the dockerin/cohesin interaction Biochemistry 38 1999 12822 12832
    • (1999) Biochemistry , vol.38 , pp. 12822-12832
    • Fierobe, H.P.1    Pages, S.2    Belaich, A.3    Champ, S.4    Lexa, D.5    Belaich, J.P.6
  • 37
    • 0030588690 scopus 로고    scopus 로고
    • Expression, purification and crystallization of a cohesin domain from the cellulosome of Clostridium thermocellum
    • Yaron S., Shimon L.J., Frolow F., Lamed R., Morag E., Shoham Y., and Bayer E.A. Expression, purification and crystallization of a cohesin domain from the cellulosome of Clostridium thermocellum J. Biotechnol. 51 1996 243 249
    • (1996) J. Biotechnol. , vol.51 , pp. 243-249
    • Yaron, S.1    Shimon, L.J.2    Frolow, F.3    Lamed, R.4    Morag, E.5    Shoham, Y.6    Bayer, E.A.7
  • 38
    • 76549203762 scopus 로고
    • A submicrodetermination of glucose
    • Park J.T., and Johnson M.J. A submicrodetermination of glucose J. Biol. Chem. 181 1949 149 151
    • (1949) J. Biol. Chem. , vol.181 , pp. 149-151
    • Park, J.T.1    Johnson, M.J.2
  • 40
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 41
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernado P., Mylonas E., Petoukhov M.V., Blackledge M., and Svergun D.I. Structural characterization of flexible proteins using small-angle X-ray scattering J. Am. Chem. Soc. 129 2007 5656 5664
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 42
    • 0029185933 scopus 로고
    • CRYSOL - A program to evalutae x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D., Barberato C., and Koch M.H.J. CRYSOL - a program to evalutae x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 43
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 44
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2


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