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Interaction of Arabidopsis kinesin-like calmodulin-binding protein with tubulin subunits: modulation by Ca2+-calmodulin by Soma B. Narasimhulu; Yu-Lin Kao; A.S.N. Reddy is a Agricultural and Biological Sciences article available to read on EtoBox.
What is Interaction of Arabidopsis kinesin-like calmodulin-binding protein with tubulin subunits: modulation by Ca2+-calmodulin about?
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+)-calmodulin. The results show that the carboxy-terminal part of the KCBP, with or without calmodulin-binding domain, binds to tubulin subunits and this binding is sensitive to nucleotides. In the presence of Ca(2+)-calmodulin the motor with calmodulin-binding domain does not bind to tubulin. This Ca(2+)-calmodulin modulation is abolished in the presence of antibodies specific to the calmodulin-binding domain of KCBP. Similar binding studies with the carboxy-terminal part of KCBP lacking the calmodulin-binding domain show no effect of Ca(2+)-calmodulin. These results indicate that Ca(2+)-calmodulin modulates the interaction of KCBP with tubulin subunits and this modulation is due to the calmodulin-binding domain in the KCBP. Calcium-dependent calmodulin modulation of KCBP interaction with tu
Who reads Interaction of Arabidopsis kinesin-like calmodulin-binding protein with tubulin subunits: modulation by Ca2+-calmodulin?
It is typically read by researchers, students, and practitioners in Agricultural and Biological Sciences.
- Author
- Soma B. Narasimhulu; Yu-Lin Kao; A.S.N. Reddy
- Publisher
- John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0960-7412)
- Published
- 1998
- Language
- EN
- Field
- Agricultural and Biological Sciences (Life Sciences)
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