The cellulolytic system of Clostridium cellulolyticum.
Recent findings on the cellulolytic system of the mesophilic Clostridium cellulolyticum are reviewed. Six cellulases and the scaffolding protein, which are, at the present time, the known components of the cellulosome have been cloned. The catalytic and structural properties of the cloned enzymes CelA, CelC, CelD and CelF are described. It was shown that the grafting of the cellulases onto the scaffolding protein was performed using the dockerin-cohesin attachment device and was strictly dependent on the integrity of both components of the complex. The amino-acid sequences of dockerin and cohesin domains of C. cellulolyticum were compared to that of C. cellulovorans and C. thermocellum. This sequence analysis shows that domains belonging to the thermophilic or the mesophilic bacteria can be placed into two well defined groups. The genetic organization of the gene cluster of C. cellulolyticum is discussed.
Bélaich
J P
JP
Bioénergétique et Ingénierie des Proteines, IBSM, Centre National de la Recherche Scientifique, Marseille, France. belaich@ibsm.cnrs-mrs.fr
Tardif
C
C
Bélaich
A
A
Gaudin
C
C
D000595:Amino Acid Sequence; D002480:Cellulase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003013:Clostridium / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data
D002480:Cellulase