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A more recent version of this article appeared on November 5, 2004 Originally published In Press as doi:10.1074/jbc.M409422200 on September 29, 2004
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Papers In Press, published online ahead of print September 9, 2004
J. Biol. Chem, 10.1074/jbc.M409422200
Submitted on August 17, 2004
Revised on September 2, 2004
Accepted on September 9, 2004

Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B

Betsy L. Lytle, Francis C. Peterson, Shi-Hong Qiu, Ming Luo, Qin Zhao, John L. Markley, and Brian F. Volkman

biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226

Corresponding Author: bvolkman{at}mcw.edu

Proper folding and assembly of tubulin aß-heterodimers involves a stepwise progression mediated by a group of protein cofactors A through E. Upon release of the tubulin monomers from the chaperonin CCT, they are acted upon by each cofactor in the folding pathway through a unique combination of protein interaction domains. Three-dimensional structures have previously been reported for cofactor A and the C-terminal CAP-Gly domain of cofactor B (CoB). Here we report the NMR structure of the N-terminal domain of Caenorhabditis elegans CoB, and show that it closely resembles ubiquitin as was recently postulated on the basis of bioinformatic analysis [Grynberg, M., Jaroszewski, L., and Godzik, A. (2003) BMC Bioinformatics 4, 46]. CoB binds partially folded a-tubulin monomers, and a putative tubulin-binding motif within its N-terminal domain was identified from sequence and structure comparisons. On the basis of molecular modeling, we hypothesize that CoB may associate with its cofactor E through association of their homologous beta-grasp domains in a manner analogous to the PB1 and CAD superfamily of protein interaction domains.


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