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J Mol Biol. 1995 Sep 15;252(2):157-62.

Heterodimerization of the two motor subunits of the heterotrimeric kinesin, KRP85/95.

Author information

1
Section of Molecular and Cellular Biology, University of California, Davis 95616, USA.

Abstract

The heterotrimeric kinesin-related motor protein, KRP85/95 is assembled from two kinesin-related polypeptides, SpKRP85 and SpKRP95, together with an uncharacterized 115 kDa polypeptide. Here we report the deduced amino acid sequence of SpKRP95, a close relative of SpKRP85. Both SpKRP85 and SpKRP95 are predicted to have a tripartite domain organization consisting of an N-terminal motor domain, a central stalk domain capable of coiled-coil formation, and a second globular C-terminal domain. The sequences of the central stalk domains predict that SpKRP85 and SpKRP95 should be capable of forming heterodimeric coiled coils. Furthermore, SpKRP85-SpKRP95 complexes can be immunoprecipitated from a cell-free translation system, providing direct evidence that SpKRP85 and SpKRP95 are capable of heterodimerization.

PMID:
7674298
DOI:
10.1006/jmbi.1995.0484
[Indexed for MEDLINE]

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