Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis

The cohesin-dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article (Pages et al., Proteins 1997;29:517-527) we predicted that four amino acid residues of the ~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 residues, whereby the species-specificity of the cohesin-dockerin interaction was altered. The results support the premise that the four residues indeed play a role in biorecognition, while additional residues may also contribute to the specificity of the interaction. (C) 2000 Wiley-Liss, Inc.