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Journal of Bacteriology, March 2007, p. 2300-2309, Vol. 189, No. 6
0021-9193/07/$08.00+0     doi:10.1128/JB.00917-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Enzyme Diversity of the Cellulolytic System Produced by Clostridium cellulolyticum Explored by Two-Dimensional Analysis: Identification of Seven Genes Encoding New Dockerin-Containing Proteins{triangledown}

Jean-Charles Blouzard,1 Caroline Bourgeois,1 Pascale de Philip,1,2 Odile Valette,1 Anne Bélaïch,1 Chantal Tardif,1,2 Jean-Pierre Bélaïch,1,2 and Sandrine Pagès1,2*

Laboratoire de Bioénergétique et Ingénierie des Protéines, IBSM, Centre National de la Recherche Scientifique,1 Université de Provence, Marseille, France2

Received 26 June 2006/ Accepted 11 December 2006

The enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum grown on crystalline cellulose as a sole carbon and energy source was explored by two-dimensional electrophoresis. The cellulolytic system of C. cellulolyticum is composed of at least 30 dockerin-containing proteins (designated cellulosomal proteins) and 30 noncellulosomal components. Most of the known cellulosomal proteins, including CipC, Cel48F, Cel8C, Cel9G, Cel9E, Man5K, Cel9M, and Cel5A, were identified by using two-dimensional Western blot analysis with specific antibodies, whereas Cel5N, Cel9J, and Cel44O were identified by using N-terminal sequencing. Unknown enzymes having carboxymethyl cellulase or xylanase activities were detected by zymogram analysis of two-dimensional gels. Some of these enzymes were identified by N-terminal sequencing as homologs of proteins listed in the NCBI database. Using Trap-Dock PCR and DNA walking, seven genes encoding new dockerin-containing proteins were cloned and sequenced. Some of these genes are clustered. Enzymes encoded by these genes belong to glycoside hydrolase families GH2, GH9, GH10, GH26, GH27, and GH59. Except for members of family GH9, which contains only cellulases, the new modular glycoside hydrolases discovered in this work could be involved in the degradation of different hemicellulosic substrates, such as xylan or galactomannan.

* Corresponding author. Mailing address: Centre National de la Recherche Scientifique, IBSM, UPR 9036, Laboratoire de Bioénergétique et Ingénierie des Protéines, 31 chemin Joseph Aiguier, 13402 Marseille, cedex 20, France. Phone: 33 4 91 16 45 47. Fax: 33 4 91 71 33 21. E-mail: pages{at}ibsm.cnrs-mrs.fr.

{triangledown} Published ahead of print on 5 January 2007.

Journal of Bacteriology, March 2007, p. 2300-2309, Vol. 189, No. 6
0021-9193/07/$08.00+0     doi:10.1128/JB.00917-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Abdou, L., Boileau, C., de Philip, P., Pages, S., Fierobe, H.-P., Tardif, C. (2008). Transcriptional Regulation of the Clostridium cellulolyticum cip-cel Operon: a Complex Mechanism Involving a Catabolite-Responsive Element. J. Bacteriol. 190: 1499-1506 [Abstract] [Full Text]  
  • Mingardon, F., Chanal, A., Tardif, C., Bayer, E. A., Fierobe, H.-P. (2007). Exploration of New Geometries in Cellulosome-Like Chimeras. Appl. Environ. Microbiol. 73: 7138-7149 [Abstract] [Full Text]  


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