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Cho, Moo Je
Ulsan National Institute of Science and Technology
Research Interests
  • Calcium Signaling
  • Calmodulin
  • Plant Defense Mechanism

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Competitive binding of calmodulin isoforms to calmodulin-binding proteins: implication for the function of calmodulin isoforms in plants

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dc.contributor.author Lee, SH ko
dc.contributor.author Kim, MC ko
dc.contributor.author Heo, WD ko
dc.contributor.author Kim, JC ko
dc.contributor.author Chung, WS ko
dc.contributor.author Park, Chan Young ko
dc.contributor.author Park, HC ko
dc.contributor.author Cheong, YH ko
dc.contributor.author Kim, CY ko
dc.contributor.author Lee, SH ko
dc.contributor.author Lee, KJ ko
dc.contributor.author Bahk, JD ko
dc.contributor.author Lee, SY ko
dc.contributor.author Cho, Moo Je ko
dc.date.available 2014-09-23T07:04:50Z -
dc.date.created 2014-09-22 ko
dc.date.issued 1999-08 ko
dc.identifier.citation BIOCHIMICA ET BIOPHYSICA ACTA - PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, v.1433, no.1-2, pp.56 - 67 ko
dc.identifier.issn 0167-4838 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/6361 -
dc.description.abstract In plants, multiple calmodulin (CaM) isoforms exist in an organism which vary in their primary structures in as much as 32 residues out of their 148 amino acids. These CaM isoforms show differences in their expression patterns and/or target enzyme activation ability. To further understand the biological significance of CaM isoforms, we examined whether CaM isoforms act on specific regulatory targets. In gel overlay assays on various soybean tissue extracts, surprisingly, two soybean CaM isoforms (SCaM-1 and SCaM-4) did not show significant differences in their target binding protein profiles, although they exhibited minor differences in their relative target binding affinities. In addition, both SCaM isoforms not only effectively bound five known plant CaMBPs, but also showed competitive binding to these proteins. Finally, immunolocalization experiments with the SCaM proteins in sections of various tissues using specific antibodies revealed similar distribution patterns for the SCaM isoforms except for root tissues, which indicates that the SCaM isoforms are concomitantly expressed in most plant tissues. These results suggest that CaM isoforms may compete for binding to CaMBPs in vivo. This competitive nature of CaM isoforms may allow modulation of Ca2+/CaM signaling pathways by virtue of relative abundance and differential target activation potency. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher Elsevier BV ko
dc.title Competitive binding of calmodulin isoforms to calmodulin-binding proteins: implication for the function of calmodulin isoforms in plants ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0032813204 ko
dc.identifier.wosid 000082296100005 ko
dc.type.rims ART ko
dc.description.wostc 39 *
dc.description.scopustc 39 *
dc.date.tcdate 2015-05-06 *
dc.date.scptcdate 2014-09-22 *
dc.identifier.doi 10.1016/S0167-4838(99)00149-1 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0032813204 ko
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