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Journal of Bacteriology, February 2003, p. 1092-1096, Vol. 185, No. 3
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.3.1092-1096.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

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

Fabrice Sabathé and Philippe Soucaille*

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 Kd 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.

* Corresponding author. Mailing address: Centre de Bioingénierie Gilbert Durand, UMR-CNRS 5504, Lab. Ass. INRA, Institut National des Sciences Appliquées, 135 avenue de Rangueil, 31077 Toulouse, France. Phone: 33 (0) 561 559 452. Fax: 33 (0) 561 559 400. E-mail: soucaille{at}insa-tlse.fr.

{dagger} For a commentary on this article, see page 701 in this issue.

Journal of Bacteriology, February 2003, p. 1092-1096, Vol. 185, No. 3
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.3.1092-1096.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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