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Journal of Bacteriology, March 2001, p. 1945-1953, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.1945-1953.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Cellulosomal Scaffoldin-Like Proteins from Ruminococcus flavefaciens

Shi-You Ding,1,2,dagger Marco T. Rincon,3 Raphael Lamed,2 Jennifer C. Martin,3 Sheila I. McCrae,3 Vincenzo Aurilia,4 Yuval Shoham,5 Edward A. Bayer,1,* and Harry J. Flint3

Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot,1 Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv,2 and Department of Food Engineering and Biotechnology, and Institute of Catalysis Science and Technology, Technion---Israel Institute of Technology, Haifa,5 Israel; Gut Microbiology Group, Rowett Research Institute, Aberdeen, United Kingdom3; and CNR-IABBAM, Ponticelli-Naples, Italy4

Received 5 September 2000/Accepted 14 December 2000

Two tandem cellulosome-associated genes were identified in the cellulolytic rumen bacterium, Ruminococcus flavefaciens. The deduced gene products represent multimodular scaffoldin-related proteins (termed ScaA and ScaB), both of which include several copies of explicit cellulosome signature sequences. The scaB gene was completely sequenced, and its upstream neighbor scaA was partially sequenced. The sequenced portion of scaA contains repeating cohesin modules and a C-terminal dockerin domain. ScaB contains seven relatively divergent cohesin modules, two extremely long T-rich linkers, and a C-terminal domain of unknown function. Collectively, the cohesins of ScaA and ScaB are phylogenetically distinct from the previously described type I and type II cohesins, and we propose that they define a new group, which we designated here type III cohesins. Selected modules from both genes were overexpressed in Escherichia coli, and the recombinant proteins were used as probes in affinity-blotting experiments. The results strongly indicate that ScaA serves as a cellulosomal scaffoldin-like protein for several R. flavefaciens enzymes. The data are supported by the direct interaction of a recombinant ScaA cohesin with an expressed dockerin-containing enzyme construct from the same bacterium. The evidence also demonstrates that the ScaA dockerin binds to a specialized cohesin(s) on ScaB, suggesting that ScaB may act as an anchoring protein, linked either directly or indirectly to the bacterial cell surface. This study is the first direct demonstration in a cellulolytic rumen bacterium of a cellulosome system, mediated by distinctive cohesin-dockerin interactions.

* Corresponding author. Mailing address: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel. Phone: (972) 8-934-2373. Fax: (972) 8-946-8256. E-mail: bfbayer{at}wicc.weizmann.ac.il.

dagger Present address: National Renewable Energy Laboratory, Biotechnology Center for Fuels & Chemicals, Golden, CO 80401.

Journal of Bacteriology, March 2001, p. 1945-1953, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.1945-1953.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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