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DC Field | Value | Language |
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dc.citation.endPage | 306 | - |
dc.citation.startPage | 299 | - |
dc.citation.title | BIOCHEMICAL JOURNAL | - |
dc.citation.volume | 350 | - |
dc.contributor.author | Lee, SH | - |
dc.contributor.author | Johnson, JD | - |
dc.contributor.author | Walsh, MP | - |
dc.contributor.author | Van Lierop, JE | - |
dc.contributor.author | Sutherland, C | - |
dc.contributor.author | Xu, AD | - |
dc.contributor.author | Snedden, WA | - |
dc.contributor.author | Kosk-Kosicka, D | - |
dc.contributor.author | Fromm, H | - |
dc.contributor.author | Narayanan, N | - |
dc.contributor.author | Cho, Moo Je | - |
dc.date.accessioned | 2023-12-22T12:07:10Z | - |
dc.date.available | 2023-12-22T12:07:10Z | - |
dc.date.created | 2014-09-23 | - |
dc.date.issued | 2000-08 | - |
dc.description.abstract | Multiple calmodulin (CaM) isoforms are expressed in plants, but their biochemical characteristics are not well resolved. Here we show the differential regulation exhibited by two soya bean CaM isoforms (SCaM-1 and SCaM-4) for the activation of five CaM-dependent enzymes, and the Ca2+ dependence of their target enzyme activation. SCaM-1 activated myosin light-chain kinase as effectively as brain CaM (K-aet 1.8 and 1.7 nM respectively), but SCaM-4 produced no activation of this enzyme. Both CaM isoforms supported near maximal activation of CaM-dependent protein kinase II (CaM KII), but SCaM-4 exhibited approx.12-fold higher K-aet than SCaM-1 for CaM KII phosphorylation of caldesmon. The SCaM isoforms showed differential activation of plant and animal Ca2+-ATPases. The plant Ca2+-ATPase was activated maximally by both isoforms, while the erythrocyte Ca2+-ATPase was activated only by SCaM-1. Plant glutamate decarboxylase was activated fully by SCaM-1, but SCaM-4 exhibited an approx. 4-fold increase in K-aet and an approx. 25 % reduction in V-max. Importantly, SCaM isoforms showed a distinct Ca2+ concentration requirement for target enzyme activation. SCaM-4 required 4-fold higher [Ca2+] for half-maximal activation of CaM KII, and 1.5-fold higher [Ca2+] for activation of cyclic nucleotide phosphodiesterase than SCaM-1. Thus these plant CaM isoforms provide a mechanism by which a different subset of target enzymes could be activated or inhibited by the differential expression of these CaM isoforms or by differences in Ca2+ transients. | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL JOURNAL, v.350, pp.299 - 306 | - |
dc.identifier.doi | 10.1042/0264-6021:3500299 | - |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.scopusid | 2-s2.0-0034663566 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/6297 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0034663566 | - |
dc.identifier.wosid | 000089067100037 | - |
dc.language | 영어 | - |
dc.publisher | PORTLAND PRESS LTD | - |
dc.title | Differential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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