Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components.
The function of the non-catalytic, duplicated segment found in C. thermocellum cellulases was investigated. Rabbit antibodies reacting with the duplicated segment of endoglucanase CelD cross-reacted with a variety of cellulosome components ranging between 50 and 100 kDa. 125I-labeled forms of CelD and of xylanase XynZ carrying the duplicated segment bound to a set of cellulosome proteins ranging between 66 and 250 kDa, particularly to the 250 kDa SL (or S1) subunit. 125I-labeled forms of CelD and XynZ devoid of the duplicated segment failed to bind to any cellulosome protein. The duplicated segment appears thus to serve to anchor the various cellulosome subunits to the complex by binding to SL, which may be a scaffolding element of the cellulosome.
Unité de Physiologie Cellulaire, Institut Pasteur, Paris, France.
K
K
Tokatlidis
S
S
Salamitou
P
P
Béguin
P
P
Dhurjati
J P
JP
Aubert
D000818:Animals; D000942:Antigens, Bacterial / Q000737:chemistry / Q000276:immunology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000276:immunology; D002474:Cell-Free System; D002480:Cellulase / Q000235:genetics*; D003013:Clostridium / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D005810:Multigene Family; D011487:Protein Conformation; D011817:Rabbits
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D002480:Cellulase