Abstract
We report the single-contig genome sequence of the anaerobic, mesophilic, cellulolytic bacterium, Bacteroides cellulosolvens. The bacterium produces a particularly elaborate cellulosome system, wherein the types of cohesin-dockerin interactions are opposite of other known cellulosome systems: cell-surface attachment is thus mediated via type-I interactions, whereas enzymes are integrated via type-II interactions.
Highlights
We report the single-contig genome sequence of the anaerobic, mesophilic, cellulolytic bacterium, Bacteroides cellulosolvens
The cellulosome is one of the most efficient systems known to biodegrade plant cell-wall polysaccharides and cellulosic wastes. This multi-enzyme extracellular complex incorporates multiple hydrolytic enzymes onto the bacterial cell-surface through dockerin modules that tightly bind to scaffoldin proteins via complementary cohesin modules [1,2,3]
Cellulosome-like complexes were further identified in the bacterium [17], supported by the recognition of the major scaffoldin protein (CipBc, later renamed ScaA) [18, 19], which includes eleven type-II cohesin domains, a family-3a carbohydrate-binding modules (CBM), and a C-terminal dockerin domain
Summary
We report the single-contig genome sequence of the anaerobic, mesophilic, cellulolytic bacterium, Bacteroides cellulosolvens. The cellulosome is one of the most efficient systems known to biodegrade plant cell-wall polysaccharides and cellulosic wastes. This multi-enzyme extracellular complex incorporates multiple hydrolytic enzymes onto the bacterial cell-surface through dockerin modules that tightly bind to scaffoldin proteins via complementary cohesin modules [1,2,3].
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