earticle

영어

Cellulosomes are cellulolytic complexes formed by highly specific interaction between one of the cohesin modules present in the scaffolding protein and a dockerin module of the catalytic components. Cellulosomal enzymes produced by C. cellulovorans grown on different carbon sources, such as Avicel, xylan, and AXP [Avicel : xylan : pectin (3:1:1)], were separated by two-dimensional electrophoresis. Using fluorescently labeled cohesin domains as described, the cohesin domains, which differ by about 58.3% in their primary structures, showed different binding profiles to the cellulosomal subunits. Fluorescence intensities of the fluorescently labeled cohesin-dockerin interactions involving cohesin6 and cohesin9 with EngY and XynB were similar, whereas EngE and EngH showed different intensities (by 1.5- to 6-fold). An enzyme-linked interaction assay showed that EngE bound preferentially to the cohesin6 comparing to cohesin9, while XynB and ManA preferences were similar. In conclusion, cohesin6 and cohesin9 showed that different binding pattern with the cellulosomal subunits under different culture conditions, it suggested cohesin-dockerin interactions occurred in a non-random fashion.