Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis

Adva Mechaly, Sima Yaron, Raphael Lamed, Henri Pierre Fierobe, Anne Belaich, Jean Pierre Belaich, Yuval Shoham, Edward A. Bayer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)170-177
Number of pages8
JournalProteins: Structure, Function and Genetics
Issue number2
StatePublished - 1 May 2000


  • Cellulases
  • Cellulosome
  • Clostridium cellulolyticum
  • Clostridium thermocellum
  • Multi-enzyme complex
  • Protein- protein interaction
  • Scaffoldin subunit


Dive into the research topics of 'Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis'. Together they form a unique fingerprint.

Cite this