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Microbiology 149 (2003), 515-524; DOI  10.1099/mic.0.25959-0
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Microbiology 149 (2003), 515-524; DOI  10.1099/mic.0.25959-0
© 2003 Society for General Microbiology

Two new cellulosome components encoded downstream of celI in the genome of Clostridium thermocellum: the non-processive endoglucanase CelN and the possibly structural protein CseP

Vladimir V. Zverlov1, Galina A. Velikodvorskaya1 and Wolfgang H. Schwarz2

1 Institute of Molecular Genetics, Russian Academy of Science, Kurchatov Sq., 123182 Moscow, Russia
2 Research Group Microbial Biotechnology, Technische Universität München, Am Hochanger 4, D-85350 Freising-Weihenstephan, Germany

Correspondence
Wolfgang H. Schwarz
schwarz{at}mikro.biologie.tu-muenchen.de

Clostridium thermocellum produces a great number of extracellular cellulases which are free or cellulosome-bound. The nucleotide sequence of a gene cluster containing the genes celI, celN and cseP was determined from C. thermocellum strain F7. Gene products Cel9I and Cel9N are structurally related enzymes having a glycosyl hydrolase family 9 and a carbohydrate-binding module (CBM3c), but show characteristic differences: Cel9I is a non-cellulosomal protein with an additional CBM (CBM3b), whereas Cel9N contains a cellulosomal dockerin module and no additional CBM. Although Cel9I is a processive endoglucanase, Cel9N is non-processive. Both enzymes hydrolyse phosphoric acid swollen cellulose, but the products of hydrolysis are different. The CseP protein encoded in the gene cluster is the first component attached to the cellulosomal scaffoldin for which no catalytic activity could be detected. It was shown to be present in the cellulosome. Its sequence is homologous to the spore-coat assembly protein CotH of Bacillus subtilis, suggesting a structural role of CseP in the cellulosome.


Abbreviations: CBM, carbohydrate-binding module; GHF, glycosyl hydrolase family; PASC, phosphoric acid swollen cellulose; pNP-, p-nitrophenyl-

The GenBank accession number for the sequence reported in this paper is AJ275974.




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