Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis

The cohesin-dockerin interaction provides the basis for incorporation of th e individual enzymatic subunits into the cellulosome complex, In a previous article (Pages et al,, Proteins 1997;29:517-527) we predicted that four am ino acid residues of the similar to 70-residue dockerin domain would serve as recognition codes for binding to the cohesin domain. The validity of the prediction was examined by site-directed mutagenesis of the suspected resi dues, whereby the species-specificity of the cohesin-dockerin interaction w as altered. The results support the premise that the four residues indeed p lay a role in biorecognition, while additional residues may also contribute to the specificity of the interaction, Proteins 2000;39:170-177. (C) 2000 Wiley-Liss, Inc.