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Journal of Bacteriology, January 2004, p. 253-257, Vol. 186, No. 1
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.1.253-257.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
H.-P. Fierobe,1 C. Tardif,1,2 F. Sabathe,3 J.-P. Belaich,1,2 and A. Belaich1*
Laboratoire de Bioénergétique et Ingénierie des Protéines, IBSM, Centre National de la Recherche Scientifique,1 Université de Provence, Marseille,2 Centre de Bioingénierie Gilbert Durand, Institut National des Sciences Appliquées, Toulouse, France3
Received 23 May 2003/ Accepted 1 October 2003
Clostridium acetobutylicum ATCC 824 converts sugars and various polysaccharides into acids and solvents. This bacterium, however, is unable to utilize cellulosic substrates, since it is able to secrete very small amounts of cellulosomes. To promote the utilization of crystalline cellulose, the strategy we chose aims at producing heterologous minicellulosomes, containing two different cellulases bound to a miniscaffoldin, in C. acetobutylicum. A first step toward this goal describes the production of miniCipC1, a truncated form of CipC from Clostridium cellulolyticum, and the hybrid scaffoldin Scaf 3, which bears an additional cohesin domain derived from CipA from Clostridium thermocellum. Both proteins were correctly matured and secreted in the medium, and their various domains were found to be functional.
Present address: Laboratoire de Biodépollution et Valorisation des Effluents Gazeux, Institut de Recherche pour le Développement, Marseille, France.
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