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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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Differential activation of NAD kinase by plant calmodulin isoforms - The critical role of domain I

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dc.contributor.author Lee, SH ko
dc.contributor.author Seo, HY ko
dc.contributor.author Kim, JC ko
dc.contributor.author Heo, WD ko
dc.contributor.author Chung, WS ko
dc.contributor.author Lee, KJ ko
dc.contributor.author Kim, MC ko
dc.contributor.author Cheong, YH ko
dc.contributor.author Choi, JY ko
dc.contributor.author Lim, CO ko
dc.contributor.author Cho, Moo Je ko
dc.date.available 2014-09-23T07:01:59Z -
dc.date.created 2014-09-19 ko
dc.date.issued 1997-04 ko
dc.identifier.citation JOURNAL OF BIOLOGICAL CHEMISTRY, v.272, no.14, pp.9252 - 9259 ko
dc.identifier.issn 0021-9258 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/6321 -
dc.description.abstract NAD kinase is a Ca2+/calmodulin (CaM)-dependent enzyme capable of converting cellular NAD to NADP. The enzyme purified from pea seedlings can be activated by highly conserved soybean CaM, SCaM-1, but not by the divergent soybean CaM isoform, SCaM-4 (Lee, S. H., Kim, J. C., Lee, M. S., Heo, W. D., Seo, H. Y., Yoon, H. W., Hong, J. C., Lee, S. Y., Bahk, J. D., Hwang, I., and Cho, M. J. (1995) J. Biol. Chem. 270, 21806-21812). To determine which domains were responsible for this differential activation of NAD kinase, a series of chimeric SCaMs were generated by exchanging functional domains between SCaM-4 and SCaM-1. SCaM-4111, a chimeric SCaM-1 that contains the first domain of SCaM-4, was severely impaired (only 40% of maximal) in its ability to activate NAD kinase. SCaM-1444, a chimeric SCaM-4 that contains the first domain of SCaM-1 exhibited nearly full (~70%) activation of NAD kinase. Only chimeras containing domain I of SCaM-1 produced greater than half-maximal activation of NAD kinase. To define the amino acid residue(s) in domain I that were responsible for this differential activation, seven single residue substitution mutants of SCaM-1 were generated and tested for NAD kinase activation. Among these mutants, only K30E and G40D showed greatly reduced NAD kinase activation. Also a double residue substitution mutant, K30E/G40D, containing these two mutations in combination was severely impaired in its NAD kinase-activating potential, reaching only 20% of maximal activation. Furthermore, a triple mutation, K30E/M36I/G40D, completely abolished NAD kinase activation. Thus, our data suggest that domain I of CaM plays a key role in the differential activation of NAD kinase exhibited by SCaM-1 and SCaM-4. Further, the residues Lys30 and Glu40 of SCaM-1 are critical for this function. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC ko
dc.title Differential activation of NAD kinase by plant calmodulin isoforms - The critical role of domain I ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0001281471 ko
dc.identifier.wosid A1997WU03700064 ko
dc.type.rims ART ko
dc.description.wostc 54 *
dc.description.scopustc 54 *
dc.date.tcdate 2015-05-06 *
dc.date.scptcdate 2014-09-19 *
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0001281471 ko
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