Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain

Sandrine Pagès, Anne Bélaïch, Jean Pierre Bélaïch, Ely Morag, Raphael Lamed, Yuval Shoham, Edward A. Bayer

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)517-527
Number of pages11
JournalProteins: Structure, Function and Genetics
Volume29
Issue number4
DOIs
StatePublished - 1997

Keywords

  • Cellulases
  • Cellulosome
  • Cohesin domain
  • EF-hand motif
  • Molecular modeling
  • Scaffoldin subunit

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