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Papers In Press, published online ahead of print April 4, 2001
Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100
Corresponding Author: Ed.Bayer{at}weizmann.ac.il
Defined chimeric cellulosomes were produced, in which selected enzymes were incorporated in specific locations within a multi-component complex. The molecular building blocks of this approach are based on complementary protein modules from the cellulosomes of two clostridia — Clostridium thermocellum and Clostridium cellulolyticum — wherein cellulolytic enzymes are incorporated into the complexes by means of high-affinity species-specific cohesin-dockerin interactions. To construct the desired complexes, a series of chimeric scaffoldins was prepared by recombinant means. The scaffoldin chimeras were designed to include two cohesin modules from the different species, optionally connected to a cellulose-binding domain. The two divergent cohesins exhibited distinct specificities, such that each recognized selectively and bound strongly to its dockerin counterpart. Using this strategy, appropriate dockerin-containing enzymes could be assembled, precisely and by design, into a desired complex. Compared to the mixture of free cellulases, the resultant cellulosome chimeras exhibited enhanced synergistic action on crystalline cellulose.
J. Biol. Chem, 10.1074/jbc.M102082200
Submitted on March 8, 2001
Revised on April 3, 2001
Accepted on April 4, 2001
Design and production of active cellulosome chimeras: Selective incorporation of dockerin-containing enzymes into defined functional complexes
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