by National Aeronautics and Space Administration, National Technical Information Service, distributor in [Washington, DC, Springfield, Va .
Written in English
|Other titles||Novel kinesin like protein with a calmodulin binding domain.|
|Statement||W. Wang ... [et al.].|
|Series||[NASA contractor report] -- NASA-CR-204645., NASA contractor report -- NASA CR-204645.|
|Contributions||Wang, W., United States. National Aeronautics and Space Administration.|
|The Physical Object|
A novel kinesin-like protein with a calmodulin-binding domain / 87 - (' 3 W. Wang 1, D. Takezawa 1, S. B. Narasimhulu 2, A. S. N. Reddy 2 and B. W. Poovaiah 1,, 1Laboratory of Plant Molecular Biology and Physiology, Department of Horticulture, Wash#Tgton State. Calcium regulates diverse developmental processes in plants through the action of calmodulin. A cDNA expression library from developing anthers of tobacco was screened with 35S-labeled calmodulin to isolate cDNAs encoding calmodulin-binding proteins. Among several clones isolated, a kinesin-like gene (TCK1) that encodes a calmodulin-binding kinesin-like protein was Cited by: Calmodulin, a ubiquitous calcium-binding protein, regulates many diverse cellular functions by modulating the activity of the proteins that interact with it. Here, we report isolation of a cDNA encoding a novel kinesin-like calmodulin-binding protein (KCBP) from Arabidopsis using biotinylated calmodulin as a probe. The coiled-coil region is coded by exons 10–15 and the conserved motor domain is coded by exons 16– The calmodulin binding domain unique to KCBP is coded by the last exon. This suggests that KCBP may have evolved by fusion of an exon coding for a calmodulin-binding domain with a kinesin-like protein by:
CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Calmodulin, a ubiquitous calcium-binding protein, regulates many diverse cellular functions by modulating the activity of the proteins that interact with it. Here, we report isolation of a cDNA encoding a novel kinesin-like calmodulin-binding protein (KCBP) from Arabidopsis using biotinylated calmodulin as a probe. Kinesin-like calmodulin-binding protein (KCBP) is a novel member of the kinesin superfamily that is involved in cell division and trichome morphogenesis. KCBP is unique among all known kinesins in having a myosin tail homology-4 region in the N-terminal tail and a calmodulin-binding region following the motor domain. Kinesin-like calmodulin-binding protein (KCBP), a novel kinesin-like protein from plants, is unique among kinesins and kinesin-like proteins in having a calmodulin-binding domain adjacent to its motor domain. KCBP localizes to mitotic microtubule (MT) arrays including the preprophase band, the spindle apparatus, and the phragmoplast, suggesting. In addition, during the purification of cardiac muscle HMWCaMBP from a Sepharose 6B column, a novel calmodulin-dependent protein kinase was discovered which has a molecular weight of 36, Da .The highly purified novel calmodulin-dependent protein kinase phosphorylated the HMWCaMBP in a Ca 2+ /calmodulin–dependent manner with the incorporation of 1 mol of .
The kinesin-like calmodulin binding protein (KCBP) is a new member of the kinesin superfamily that appears to be present only in plants. The KCBP is unique in its ability to interact with calmodulin in a Ca2-dependent manner. To study the interaction of the KCBP with microtubules, we expressed different regions of the Arabidopsis KCBP and used the purified proteins in Cited by: Get this from a library! A novel kinesin-like protein with a calmodulin-binding domain. [W Wang; United States. National Aeronautics and Space Administration.;]. Reddy AS, Safadi F, Narasimhulu SB, Golovkin M, Hu X. A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain. J Biol Chem. Mar 22; (12)– Reddy AS, Narasimhulu SB, Day IS. Structural organization of a gene encoding a novel calmodulin-binding kinesin-like protein from Arabidopsis. by: The kinesin protein Kif7 is a critical regulator of Gli transcription factors in mammalian hedgehog signaling. Sci Signal. ; 2:ra doi: /scisignal Day IS, Miller C, Golovkin M, Reddy AS. Interaction of a kinesin-like calmodulin-binding protein with a protein kinase.