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Characterization of the CipA Scaffolding Protein and In Vivo Production of a Minicellulosome in Clostridium acetobutylicum

Centre de Bioingénierie Gilbert Durand, UMR-CNRS 5504, Lab. Ass. INRA, Institut National des Sciences Appliquées, 31077 Toulouse, France

Received 22 July 2002/ Accepted 31 October 2002

The cipA gene encoding the Clostridium acetobutylicum scaffolding protein CipA was cloned and expressed in Escherichia coli. CipA contains an N-terminal signal peptide, a family 3a cellulose-binding domain (CBD), five type I cohesin domains, and six hydrophilic domains. The uniqueness of CipA lies in the enchainment of cohesin domains that are all separated by a hydrophilic domain. Affinity-purified CipA was used in equilibrium-binding experiments to characterize the interaction of CipA with crystalline cellulose. A K_d of 0.038 µM and a [C]_max of 0.43 µmol of CipA bound per g of Avicel were determined. A mini-CipA polypeptide consisting of a CBD3a and two cohesin domains was overexpressed in C. acetobutylicum, yielding the in vivo formation of a minicellulosome. This is to our knowledge the first demonstration of the in vivo assembly of a recombinant minicellulosome.

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