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Journal of Bacteriology, December 2008, p. 8220-8222, Vol. 190, No. 24
0021-9193/08/$08.00+0     doi:10.1128/JB.00609-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Cell Surface Enzyme Attachment Is Mediated by Family 37 Carbohydrate-Binding Modules, Unique to Ruminococcus albus{triangledown} ,{ddagger}

Anat Ezer,1,{dagger} Erez Matalon,1,{dagger} Sadanari Jindou,1 Ilya Borovok,1 Nof Atamna,1 Zhongtang Yu,2 Mark Morrison,2,3 Edward A. Bayer,4* and Raphael Lamed1

Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv 69978, Israel,1 MAPLE Research Initiative, Department of Animal Sciences, The Ohio State University, Columbus, Ohio,2 CSIRO Livestock Industries, St. Lucia, QLD 4068, Australia,3 Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel4

Received 1 May 2008/ Accepted 8 October 2008

The rumen bacterium Ruminococcus albus binds to and degrades crystalline cellulosic substrates via a unique cellulose degradation system. A unique family of carbohydrate-binding modules (CBM37), located at the C terminus of different glycoside hydrolases, appears to be responsible both for anchoring these enzymes to the bacterial cell surface and for substrate binding.

* 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: ed.bayer{at}weizmann.ac.il

{triangledown} Published ahead of print on 17 October 2008.

{ddagger} Supplemental material for this article may be found at http://jb.asm.org/.

{dagger} These two authors contributed equally to this work.

Journal of Bacteriology, December 2008, p. 8220-8222, Vol. 190, No. 24
0021-9193/08/$08.00+0     doi:10.1128/JB.00609-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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