Cellulosomal Scaffoldin-Like Proteins from Ruminococcus flavefaciens

doi:10.1128/JB.183.6.1945-1953.2001

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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^, 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. Thededuced gene products represent multimodular scaffoldin-relatedproteins (termed ScaA and ScaB), both of which include severalcopies of explicit cellulosome signature sequences. The scaB genewas completely sequenced, and its upstream neighbor scaA was partiallysequenced. The sequenced portion of scaA contains repeating cohesinmodules and a C-terminal dockerin domain. ScaB contains sevenrelatively divergent cohesin modules, two extremely long T-richlinkers, and a C-terminal domain of unknown function. Collectively,the cohesins of ScaA and ScaB are phylogenetically distinct fromthe previously described type I and type II cohesins, and we proposethat they define a new group, which we designated here type IIIcohesins. Selected modules from both genes were overexpressedin Escherichia coli, and the recombinant proteins were used asprobes in affinity-blotting experiments. The results stronglyindicate that ScaA serves as a cellulosomal scaffoldin-like proteinfor several R. flavefaciens enzymes. The data are supported bythe direct interaction of a recombinant ScaA cohesin with an expresseddockerin-containing enzyme construct from the same bacterium.The evidence also demonstrates that the ScaA dockerin binds toa specialized cohesin(s) on ScaB, suggesting that ScaB may actas an anchoring protein, linked either directly or indirectlyto the bacterial cell surface. This study is the first directdemonstration in a cellulolytic rumen bacterium of a cellulosomesystem, mediated by distinctive cohesin-dockerininteractions.

^* 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.

Present address: National Renewable Energy Laboratory, Biotechnology Center for Fuels & Chemicals, Golden, CO80401.

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