Community Research and Development Information Service - CORDIS

Molecular genetics of the cellulase system of Clostridium thermocellum

Clostridium thermocellum cellulase consists of a high molecular weight, multienzyme complex, termed cellulosome. Catalytic subunits of the cellulosome comprise various beta-glycanases (cellulases, xylanases, mannanases), which are anchored to a large scaffolding component termed CipA. Each of the catalytic components comprises a noncatalytic anchored domain, termed dockerin domain, which binds to a complementary domains of CipA, termed cohesin domains (interaction of type I). CipA is anchored to bacterial cell surfaces by means of a specialised dockerin domain, which binds to surface proteins harbouring a complementary, specific cohesin domain (interactions of type II). We study individual catlaytic subunits as well as interactions of type I and II, with a view to reconstitute artificial protein complexes. These may help to understand the high specific activity of the cellulosome in degrading cellulose and open the way for the design of multienzyme complexes not necessarily involved in cellulos hydrolysis.

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Institut Pasteur
28 rue du Docteur Roux
75724 Paris
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