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MeSH Review

Cellulosomes

 
 
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Disease relevance of Cellulosomes

 

High impact information on Cellulosomes

  • The resultant trifunctional designer cellulosomes were assayed on homogeneous and complex substrates (microcrystalline cellulose and straw, respectively) and found to be considerably more active than the corresponding free enzyme or bifunctional systems [4].
  • Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes [5].
  • Cohesin-dockerin interaction in cellulosome assembly: a single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition [6].
  • The cellulosomes of anaerobic fungi convert crystalline cellulose solely into glucose, in contrast with bacterial cellulosomes which produce cellobiose [7].
  • beta-Glucosidase in cellulosome of the anaerobic fungus Piromyces sp. strain E2 is a family 3 glycoside hydrolase [7].
 

Chemical compound and disease context of Cellulosomes

 

Biological context of Cellulosomes

 

Associations of Cellulosomes with chemical compounds

  • In a similar experiment with EDTA-treated cellulosomes, these subunits reacted with anti-bCDR1 but not with anti-bCDR2, showing that they lost the bCDR2 epitope and were truncated [14].
  • Hydrolytic components of the cellulosome are organized around a large, noncatalytic glycoprotein termed CipA that acts both as a scaffolding component and a cellulose-binding factor [15].
  • The intact cellulosomes hydrolyzes crystalline cellulose in the presence of Ca2+ and thiols [8].
  • The cellulosome produced by Piromyces sp. strain E2 during growth on filter paper was purified by using an optimized cellulose-affinity method consisting of steps of EDTA washing of the cellulose-bound protein followed by elution with water [16].
  • Cohesin-dockerin interaction in cellulosome assembly: a single Asp-to-Asn mutation disrupts high-affinity cohesin-dockerin binding [17].
 

Gene context of Cellulosomes

  • The gene lies between cipC (the gene encoding the cellulosome scaffolding protein) and celC (coding for the endoglucanase C) in the large cel cluster of this mesophilic cellulolytic Clostridium species [18].
  • We report here a new cellulase gene, celK, coding for CelK, a 98-kDa major component of the cellulosome [13].
  • Furthermore, evidence is presented that the NCDDs in CelC from the polycentric fungus Orpinomyces sp. strain PC-2 specifically recognize four proteins in a cellulosome preparation, indicating the presence of multiple scaffoldins [11].
  • These data show for the first time that GH family 48 cellulases are not confined to bacteria, and that bacterial and fungal cellulosomes share the same pivotal component [19].

References

  1. Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii. Irihimovitch, V., Eichler, J. J. Biol. Chem. (2003) [Pubmed]
  2. Heterologous production of Clostridium cellulovorans engB, using protease-deficient Bacillus subtilis, and preparation of active recombinant cellulosomes. Murashima, K., Chen, C.L., Kosugi, A., Tamaru, Y., Doi, R.H., Wong, S.L. J. Bacteriol. (2002) [Pubmed]
  3. Production by Clostridium acetobutylicum ATCC 824 of CelG, a cellulosomal glycoside hydrolase belonging to family 9. López-Contreras, A.M., Martens, A.A., Szijarto, N., Mooibroek, H., Claassen, P.A., van der Oost, J., de Vos, W.M. Appl. Environ. Microbiol. (2003) [Pubmed]
  4. 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., Bélaïch, A., Rincon, M.T., Pagès, S., Lamed, R., Tardif, C., Bélaïch, J.P., Bayer, E.A. J. Biol. Chem. (2005) [Pubmed]
  5. 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., Shoham, Y., Belaich, J.P., Bayer, E.A. J. Biol. Chem. (2001) [Pubmed]
  6. Cohesin-dockerin interaction in cellulosome assembly: a single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition. Mechaly, A., Fierobe, H.P., Belaich, A., Belaich, J.P., Lamed, R., Shoham, Y., Bayer, E.A. J. Biol. Chem. (2001) [Pubmed]
  7. beta-Glucosidase in cellulosome of the anaerobic fungus Piromyces sp. strain E2 is a family 3 glycoside hydrolase. Steenbakkers, P.J., Harhangi, H.R., Bosscher, M.W., van der Hooft, M.M., Keltjens, J.T., van der Drift, C., Vogels, G.D., op den Camp, H.J. Biochem. J. (2003) [Pubmed]
  8. Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of trucated polypeptides. Choi, S.K., Ljungdahl, L.G. Biochemistry (1996) [Pubmed]
  9. A major new component in the cellulosome of Clostridium thermocellum is a processive endo-beta-1,4-glucanase producing cellotetraose. Zverlov, V.V., Schantz, N., Schwarz, W.H. FEMS Microbiol. Lett. (2005) [Pubmed]
  10. Purification and characterization of an endoglucanase from the cellulosomes (multicomponent cellulase complexes) of Clostridium thermocellum. Mori, Y. Biosci. Biotechnol. Biochem. (1992) [Pubmed]
  11. Noncatalytic docking domains of cellulosomes of anaerobic fungi. Steenbakkers, P.J., Li, X.L., Ximenes, E.A., Arts, J.G., Chen, H., Ljungdahl, L.G., Op Den Camp, H.J. J. Bacteriol. (2001) [Pubmed]
  12. Substrate-induced production and secretion of cellulases by Clostridium acetobutylicum. López-Contreras, A.M., Gabor, K., Martens, A.A., Renckens, B.A., Claassen, P.A., Van Der Oost, J., De Vos, W.M. Appl. Environ. Microbiol. (2004) [Pubmed]
  13. Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination. Kataeva, I., Li, X.L., Chen, H., Choi, S.K., Ljungdahl, L.G. J. Bacteriol. (1999) [Pubmed]
  14. Structural role of calcium for the organization of the cellulosome of Clostridium thermocellum. Choi, S.K., Ljungdahl, L.G. Biochemistry (1996) [Pubmed]
  15. The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation. Béguin, P., Lemaire, M. Crit. Rev. Biochem. Mol. Biol. (1996) [Pubmed]
  16. An intron-containing glycoside hydrolase family 9 cellulase gene encodes the dominant 90 kDa component of the cellulosome of the anaerobic fungus Piromyces sp. strain E2. Steenbakkers, P.J., Ubhayasekera, W., Goossen, H.J., van Lierop, E.M., van der Drift, C., Vogels, G.D., Mowbray, S.L., Op den Camp, H.J. Biochem. J. (2002) [Pubmed]
  17. Cohesin-dockerin interaction in cellulosome assembly: a single Asp-to-Asn mutation disrupts high-affinity cohesin-dockerin binding. Handelsman, T., Barak, Y., Nakar, D., Mechaly, A., Lamed, R., Shoham, Y., Bayer, E.A. FEBS Lett. (2004) [Pubmed]
  18. Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli. Reverbel-Leroy, C., Belaich, A., Bernadac, A., Gaudin, C., Belaich, J.P., Tardif, C. Microbiology (Reading, Engl.) (1996) [Pubmed]
  19. The major component of the cellulosomes of anaerobic fungi from the genus Piromyces is a family 48 glycoside hydrolase. Steenbakkers, P.J., Freelove, A., Van Cranenbroek, B., Sweegers, B.M., Harhangi, H.R., Vogels, G.D., Hazlewood, G.P., Gilbert, H.J., Op den Camp, H.J. DNA Seq. (2002) [Pubmed]
 
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