Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP85/95

Dana J. Rashid, Karen P. Wedaman, Jonathan M. Scholey

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

The heterotrimeric kinesin-related motor protein, KRP85/95is 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, ad 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.

Original languageEnglish (US)
Pages (from-to)157-162
Number of pages6
JournalJournal of Molecular Biology
Volume252
Issue number2
DOIs
StatePublished - Sep 15 1995

Keywords

  • KRP; heterotrimeric kinesin; motor protein

ASJC Scopus subject areas

  • Molecular Biology
  • Virology

Fingerprint Dive into the research topics of 'Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP<sub>85/95</sub>'. Together they form a unique fingerprint.

  • Cite this