Heterodimerization of the two motor subunits of the heterotrimeric kinesin, KRP85/95.
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.
Rashid
D J
DJ
Section of Molecular and Cellular Biology, University of California, Davis 95616, USA.
Wedaman
K P
KP
Scholey
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry*; D010063:Ovum / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D012617:Sea Urchins; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D002135:Calcium-Binding Proteins; D009124:Muscle Proteins; D010455:Peptides; C074152:kinesin-II; D016547:Kinesins