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Analysis of heterodimer formation by Xkl ... kinesin-II from Xenopus laevis
Analysis of heterodimer formation by Xklp3A/B, a newly cloned kinesin-II from Xenopus laevis.
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kinesin-II motor proteins are composed of two different kinesin-like motor proteins and one cargo binding subunit. Here we report the cloning of a new member of the kinesin-II superfamily, Xklp3A from Xenopus laevis, which forms a heterodimeric complex with Xklp3B. The heterodimer formation properties between Xklp3A and B have been tested in vitro using reticulocyte lysate expression and immunoprecipitation. To this end we produced a series of Xklp3A and B constructs of varying length and tested their propensity for heterodimer formation. We could demonstrate that, in contrast to conventional kinesin, the critical domains for heterodimer formation in Xklp3A/B are located at the C-terminal end of the stalk. Neither the neck nor the highly charged stretches after the neck region, which are typical of kinesins-II, are required for heterodimer formation, nor do they prevent homodimer formation. Dimerization is controlled by a cooperative mechanism between the C-terminal coiled-coil segments. Classical trigger sites were not identified. The critical regions for dimerization exhibit a very high degree of sequence conservation among equivalent members of the kinesin-II family.
De Marco V, Burkhard P, Le Bot N, Vernos I, Hoenger A
The EMBO journal
2001-07-02 00:00
20
13
3370-9
Amino Acid Sequence,Animals,Calcium-Binding Proteins,Cloning, Molecular,Conserved Sequence,Dimerization,Kinesin,Models, Molecular,Molecular Sequence Data,Muscle Proteins,Protein Conformation,Recombinant Proteins,Repetitive Sequences, Amino Acid,Sequence Alignment,Sequence Homology, Amino Acid,Xenopus Proteins,Xenopus laevis,Calcium-Binding Proteins,Muscle Proteins,Recombinant Proteins,XKLP3 protein, Xenopus,Xenopus Proteins,xklp3A protein, Xenopus,kinesin-II,Kinesin
EMBL Structural and Computational Biology Programme, Meyerhofstrasse 1, 69117 Heidelberg, Germany
EMBO J.
0261-4189
10.1093/emboj/20.13.3370
550
True
11432825
