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 Citations (Scopus)

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

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Kinesin
Peptides
Cell-Free System
Amino Acid Sequence
Proteins

Keywords

  • KRP; heterotrimeric kinesin; motor protein

ASJC Scopus subject areas

  • Molecular Biology
  • Virology

Cite this

Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP85/95 . / Rashid, Dana J.; Wedaman, Karen P.; Scholey, Jonathan M.

In: Journal of Molecular Biology, Vol. 252, No. 2, 15.09.1995, p. 157-162.

Research output: Contribution to journalArticle

Rashid, Dana J. ; Wedaman, Karen P. ; Scholey, Jonathan M. / Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP85/95 In: Journal of Molecular Biology. 1995 ; Vol. 252, No. 2. pp. 157-162.
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