MBE Advance Access published online on November 20, 2007
Molecular Biology and Evolution, doi:10.1093/molbev/msm243
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Research Article |
Insight into Ligand Diversity and Novel Biological Roles for Family 32 Carbohydrate Binding Modules
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1 Department of Biochemistry and Microbiology, University of Victoria, Victoria, V8W 3P6, CANADA
2 Departamento de Biologia Celular y Molecular, Universidade da Coruña, A Coruña, E15071, SPAIN
To whom all correspondence should be addressed: Room 218 Petch Building, Department of Biochemistry and Microbiology, University of Victoria, Victoria, B.C., CAN, V8W 3P6, Tel: (250) 472-4168, Email: wabbott{at}uvic.ca
Received for publication June 22, 2007. Revision received October 11, 2007. Accepted for publication October 26, 2007.
Family 32 carbohydrate binding modules (CBM32s) are found in a diverse group of microorganisms including, archea, eubacteria and fungi. Significantly, many members of this family belong to plant and animal pathogens where they are likely to play a key role in enzyme toxin targeting and function. Indeed, ligand targets have been shown to range from insoluble plant cell wall polysaccharides to complex eukaryotic glycans. Besides a potential direct involvement in microbial l pathogenesis, CBM32s also represent an important family for the study of CBM evolution due to the wide variety of complex protein architectures that they are associated with. This complexity ranges from independent lectin-like proteins through to large multimodular enzyme toxins where they can be present in multiple copies (multimodularity). Presented here is a rigorous analysis of the evolutionary relationships between available polypeptide sequences for family 32 CBMs within the carbohydrate active enzyme (CAZy) database. This approach is especially helpful for determining the roles of CBM32s that are present in multiple copies within an enzyme as each module tends to cluster into groups that are associated with distinct enzyme classes. For enzymes that contain multiple copies of CBM32s, however, there are differential clustering patterns as modules can either cluster together or in very distant sections of the tree. These data suggest that enzymes containing multiple copies possess complex mechanisms of ligand recognition. By applying this well-developed approach to the specific analysis CBM relatedness, we have generated here a new platform for the prediction of CBM binding specificity and highlight significant new targets for biochemical and structural characterization.
Key Words: Carbohydrate Binding Module • Family 32 • Evolution • Multimodularity • Structural Characterization
* These authors contributed equally to this work.
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