The Cotton Kinesin-Like Calmodulin-Binding Protein Associates with Cortical Microtubules in Cotton Fibers
نویسندگان
چکیده
منابع مشابه
A plant-specific kinesin binds to actin microfilaments and interacts with cortical microtubules in cotton fibers.
A novel kinesin, GhKCH1, has been identified from cotton (Gossypium hirsutum) fibers. GhKCH1 has a centrally located kinesin catalytic core, a signature neck peptide of minus end-directed kinesins, and a unique calponin homology (CH) domain at its N terminus. GhKCH1 and other CH domain-containing kinesins (KCHs) belong to a distinct branch of the minus end-directed kinesin subfamily. To date th...
متن کاملA cotton kinesin GhKCH2 interacts with both microtubules and microfilaments.
Many biological processes require the co-operative involvement of both microtubules and microfilaments; however, only a few proteins mediating the interaction between microtubules and microfilaments have been identified from plants. In the present study, a cotton kinesin GhKCH2, which contains a CH (calponin homology) domain at the N-terminus, was analysed in vitro and in vivo in order to under...
متن کاملOrigin and evolution of Kinesin-like calmodulin-binding protein.
Kinesin-like calmodulin-binding protein (KCBP), a member of the Kinesin-14 family, is a C-terminal microtubule motor with three unique domains including a myosin tail homology region 4 (MyTH4), a talin-like domain, and a calmodulin-binding domain (CBD). The MyTH4 and talin-like domains (found in some myosins) are not found in other reported kinesins. A calmodulin-binding kinesin called kinesin-...
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Kinesin-like calmodulin-binding protein (KCBP) is a recently identified novel kinesin-like protein that appears to be unique to and ubiquitous in plants. KCBP is distinct from all other known KLPs in having a calmodulin-binding domain adjacent to its motor domain. We have used different regions of KCBP to study its interaction with tubulin subunits and the regulation of this interaction by Ca(2...
متن کاملStructural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein.
Kinesins are molecular motors that power cell division and transport of various proteins and organelles. Their motor activity is driven by ATP hydrolysis and depends on interactions with microtubule tracks. Essential steps in kinesin movement rely on controlled alternate binding to and detaching from the microtubules. The conformational changes in the kinesin motors induced by nucleotide and mi...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 2003
ISSN: 1532-2548,0032-0889
DOI: 10.1104/pp.103.020339