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Open Access Highly Accessed Research

Sequence and structural analysis of BTB domain proteins

Peter J Stogios1, Gregory S Downs2, Jimmy JS Jauhal1, Sukhjeen K Nandra1 and Gilbert G Privé134*

Author Affiliations

1 Department of Medical Biophysics, University of Toronto, Toronto, Ontario, M5G 2M9, Canada

2 Bioinformatics Certificate Program, Seneca College, Toronto, Ontario, M3J 3M6, Canada

3 Department of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada

4 Ontario Cancer Institute, 610 University Avenue, Toronto, Ontario, M5G 2M9, Canada

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Genome Biology 2005, 6:R82  doi:10.1186/gb-2005-6-10-r82

Published: 15 September 2005

Abstract

Background

The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination. Several BTB domain structures have been experimentally determined, revealing a highly conserved core structure.

Results

We surveyed the protein architecture, genomic distribution and sequence conservation of BTB domain proteins in 17 fully sequenced eukaryotes. The BTB domain is typically found as a single copy in proteins that contain only one or two other types of domain, and this defines the BTB-zinc finger (BTB-ZF), BTB-BACK-kelch (BBK), voltage-gated potassium channel T1 (T1-Kv), MATH-BTB, BTB-NPH3 and BTB-BACK-PHR (BBP) families of proteins, among others. In contrast, the Skp1 and ElonginC proteins consist almost exclusively of the core BTB fold. There are numerous lineage-specific expansions of BTB proteins, as seen by the relatively large number of BTB-ZF and BBK proteins in vertebrates, MATH-BTB proteins in Caenorhabditis elegans, and BTB-NPH3 proteins in Arabidopsis thaliana. Using the structural homology between Skp1 and the PLZF BTB homodimer, we present a model of a BTB-Cul3 SCF-like E3 ubiquitin ligase complex that shows that the BTB dimer or the T1 tetramer is compatible in this complex.

Conclusion

Despite widely divergent sequences, the BTB fold is structurally well conserved. The fold has adapted to several different modes of self-association and interactions with non-BTB proteins.