期刊
EMBO JOURNAL
卷 20, 期 13, 页码 3370-3379出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.13.3370
关键词
alpha-helical coiled coil; coiled-coil trigger site; heptad repeats; kinesin-II; Xklp3A/B
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 immnnoprecipitation, 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.
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