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Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis.

Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis. Research Abstract Details 

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  • Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis. Abstract Text:

    jae cheol jeongJae Cheol Jeong,dongjin shinDongjin Shin,jiyoung leeJiyoung Lee,chang ho kangChang Ho Kang,dongwon baekDongwon Baek,moo je choMoo Je Cho,min chul kimMin Chul Kim,dae-jin yunDae-Jin Yun,jae cheol jeongJae Cheol Jeong,dongjin shinDongjin Shin,jiyoung leeJiyoung Lee,chang ho kangChang Ho Kang,dongwon baekDongwon Baek,moo je choMoo Je Cho,min chul kimMin Chul Kim,dae-jin yunDae-Jin Yun,

    Protein phosphorylation is one of the major mechanisms by which eukaryotic cells transduce extracellular signals into intracellular responses. Calcium/calmodulin (Ca(2+)/CaM)-dependent protein phosphorylation has been implicated in various cellular processes, yet little is known about Ca(2+)/CaM-dependent protein kinases (CaMKs) in plants. From an Arabidopsis expression library screen using a horseradish peroxidase-conjugated soybean calmodulin isoform (SCaM-1) as a probe, we isolated a full-length cDNA clone that encodes AtCK (Arabidopsis thaliana calcium/calmodulin-dependent protein kinase). The predicted structure of AtCK contains a serine/threonine protein kinase catalytic domain followed by a putative calmodulin-binding domain and a putative Ca(2+)-binding domain. Recombinant AtCK was expressed in E. coli and bound to calmodulin in a Ca(2+)-dependent manner. The ability of CaM to bind to AtCK was confirmed by gel mobility shift and competition assays. AtCK exhibited its highest levels of autophosphorylation in the presence of 3 mM Mn(2+). The phosphorylation of myelin basic protein (MBP) by AtCK was enhanced when AtCK was under the control of calcium-bound CaM, as previously observed for other Ca(2+)/CaM-dependent protein kinases. In contrast to maize and tobacco CCaMKs (calcium and Ca(2+)/CaM-dependent protein kinase), increasing the concentration of calmodulin to more than 3 microgram suppressed the phosphorylation activity of AtCK. Taken together our results indicate that AtCK is a novel Arabidopsis Ca(2+)/CaM-dependent protein kinase which is presumably involved in CaM-mediated signaling.

    Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis. Publishing Authors By Initials

    jc jeongJC Jeong,d shinD Shin,j leeJ Lee,ch kangCH Kang,d baekD Baek,mj choMJ Cho,mc kimMC Kim,dj yunDJ Yun,jc jeongJC Jeong,d shinD Shin,j leeJ Lee,ch kangCH Kang,d baekD Baek,mj choMJ Cho,mc kimMC Kim,dj yunDJ Yun,

    For similar abstracts research abstracts see: abstracts research

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    Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Molecules and cells

    VOLUME: 24

    Page Numbers: 276-82

    Journal Abbreviation: Mol. Cells

    ISSN: 1016-8478

    DAY: 31

    MONTH: Oct

    YEAR: 2007

    Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis. Information

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    LANGUAGE: eng

    NlmUniqueID: 9610936

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    Grant and Affiliation Information for Isolation and characterization of a novel calcium/calmodulin-dependent protein kinase, AtCK, from arabidopsis.

    AFFILIATION: Division of Applied Life Sciences (BK21 program), Plant Molecular Biology & Biotechnology Research Center, Graduate School of Gyeongsang National University, Jinju 660-701, Korea.

    Country: Korea (South)

    Korea (South) Research PublicationKorea (South) Research Publication

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    MEDLINETA: Mol Cells

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