1997/12/01 by Sandrine Pagès, A. Belaich, Anne Bélaïch +6 · 3 citations
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · #Biochemical and Structural Characterization #Enzyme Production and Characterization #Polysaccharides and Plant Cell Walls
paper · pdf · doi:10.1002/(sici)1097-0134(199712)29:4<517::aid-prot11>3.0.co;2-p
openalex publication_date 1997/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
The cross-species specificity of the cohesin-dockerin interaction, which defines the incorporation of the enzymatic subunits into the cellulosome complex, has been investigated. Cohesin-containing segments from the cellulosomes of two different species, Clostridium thermocellum and Clostridium cellulolyticum, were allowed to interact with cellulosomal (dockerin-containing) enzymes from each species. In both cases, the cohesin domain of one bacterium interacted with enzymes from its own cellulosome in a calcium-dependent manner, but the same cohesin failed to recognize enzymes from the other species. Thus, in the case of these two bacteria, the cohesin-dockerin interaction seems to be species-specific. Based on intra- and cross-species sequence comparisons among the different dockerins together with their known specificities, we tender a prediction as to the amino-acid residues critical to recognition of the cohesins. The suspected residues were narrowed down to only four, which comprise a repeated pair located within the calcium-binding motif of two duplicated sequences, characteristic of the dockerin domain. According to the proposed model, these four residues do not participate in the binding of calcium per se; instead, they appear to serve as recognition codes in promoting interaction with the cohesin surface.