Journal article
A “Slow” Homotetrameric Kinesin-related Motor Protein Purified from Drosophila Embryos
The Journal of biological chemistry, Vol.269(37), pp.22913-22916
09/16/1994
Handle:
https://hdl.handle.net/2376/117262
PMCID: PMC3201834
PMID: 8083185
Abstract
Pan-kinesin peptide antibodies were used to identify and isolate kinesin-related proteins (KRPs) from
Drosophila melanogaster
embryonic cytosol. These KRPs cosedimented with microtubules (MTs) polymerized from cytosol treated with AMP-PNP (adenyl-5′-yl imidodiphosphate), and one of them, KRP
130
, was further purified from ATP eluates of the embryonic MTs. Purified KRP
130
behaves as a homotetrameric complex composed of four 130-kDa polypeptide subunits which displays a “slow” plus-end directed motor activity capable of moving single MTs at 0.04 ± 0.01 μm/s. The 130-kDa subunit of KRP
130
was tested for reactivity with monoclonal and polyclonal antibodies that are specific for various members of the kinesin superfamily. Results indicate that the KRP
130
subunit is related to
Xenopus
Eg5 (Sawin, K. E., Le Guellec, K. L., Philippe, M., Mitchinson, T. J. (1992)
Nature
359, 540-543), a member of the BimC subfamily of kinesins. Therefore, KRP
130
appears to be the first
Drosophila
KRP, and the first member of the BimC subfamily in any organism, to be purified from native a multimeric motor complex.
Metrics
10 Record Views
Details
- Title
- A “Slow” Homotetrameric Kinesin-related Motor Protein Purified from Drosophila Embryos
- Creators
- Douglas G Cole - Section of Molecular and Cellular Biology, University of California, Davis, California 95616William M Saxtonlll - Department of Biology, Institute for Molecular and Cellular Biology, Indiana University, Bloomington, Indiana 47405Kathy B Sheehan - Department of Biology, Institute for Molecular and Cellular Biology, Indiana University, Bloomington, Indiana 47405Jonathan M Scholey - Section of Molecular and Cellular Biology, University of California, Davis, California 95616
- Publication Details
- The Journal of biological chemistry, Vol.269(37), pp.22913-22916
- Academic Unit
- Center for Reproductive Biology
- Grant note
- R01 GM046295-09 || GM / National Institute of General Medical Sciences : NIGMS
- Identifiers
- 99900548143901842
- Language
- English
- Resource Type
- Journal article