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Applied and Environmental Microbiology, June 2007, p. 3536-3546, Vol. 73, No. 11
0099-2240/07/$08.00+0 doi:10.1128/AEM.00225-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Genome Sequence of the Cellulolytic Gliding Bacterium Cytophaga hutchinsonii
,
Gary Xie,1,2
David C. Bruce,1,2
Jean F. Challacombe,1,2
Olga Chertkov,1,2
John C. Detter,1,2
Paul Gilna,1,2
Cliff S. Han,1,2
Susan Lucas,2,4
Monica Misra,1
Gerald L. Myers,1
Paul Richardson,2,5
Roxanne Tapia,1,2
Nina Thayer,1
Linda S. Thompson,1,2
Thomas S. Brettin,1,2
Bernard Henrissat,3
David B. Wilson,6 and
Mark J. McBride7*
Los Alamos National Laboratory, Bioscience Division, Los Alamos, New Mexico,1
Department of Energy Joint Genome Institute, Walnut Creek, California,2
Architecture et Fonction des Macromolecules Biologiques, UMR 6098, Centre National de la Recherche Scientifique, and Universities of Aix-Marseille I and II, Marseille, France,3
Lawrence Livermore National Laboratory, Livermore, California,4
Lawrence Berkeley National Laboratory, Berkeley, California,5
Cornell University, Ithaca, New York,6
University of WisconsinMilwaukee, Milwaukee, Wisconsin7
Received 29 January 2007/
Accepted 23 March 2007
The complete DNA sequence of the aerobic cellulolytic soil bacterium Cytophaga hutchinsonii, which belongs to the phylum Bacteroidetes, is presented. The genome consists of a single, circular, 4.43-Mb chromosome containing 3,790 open reading frames, 1,986 of which have been assigned a tentative function. Two of the most striking characteristics of C. hutchinsonii are its rapid gliding motility over surfaces and its contact-dependent digestion of crystalline cellulose. The mechanism of C. hutchinsonii motility is not known, but its genome contains homologs for each of the gld genes that are required for gliding of the distantly related bacteroidete Flavobacterium johnsoniae. Cytophaga-Flavobacterium gliding appears to be novel and does not involve well-studied motility organelles such as flagella or type IV pili. Many genes thought to encode proteins involved in cellulose utilization were identified. These include candidate endo-ß-1,4-glucanases and ß-glucosidases. Surprisingly, obvious homologs of known cellobiohydrolases were not detected. Since such enzymes are needed for efficient cellulose digestion by well-studied cellulolytic bacteria, C. hutchinsonii either has novel cellobiohydrolases or has an unusual method of cellulose utilization. Genes encoding proteins with cohesin domains, which are characteristic of cellulosomes, were absent, but many proteins predicted to be involved in polysaccharide utilization had putative D5 domains, which are thought to be involved in anchoring proteins to the cell surface.
* Corresponding author. Mailing address: Department of Biological Sciences, University of WisconsinMilwaukee, 3209 N. Maryland Ave., 181 Lapham Hall, Milwaukee, WI 53211. Phone: (414) 229-5844. Fax: (414) 229-3926. E-mail:
mcbride{at}uwm.edu
Published ahead of print on 30 March 2007.
Supplemental material for this article may be found at http://aem.asm.org/.
Applied and Environmental Microbiology, June 2007, p. 3536-3546, Vol. 73, No. 11
0099-2240/07/$08.00+0 doi:10.1128/AEM.00225-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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