Rice OsERG3 encodes an unusual small C2-domain protein containing a Ca2+-binding module but lacking phospholipid-binding properties

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dc.contributor.authorC H Kang-
dc.contributor.authorB C Moon-
dc.contributor.authorH C Park-
dc.contributor.authorS C Koo-
dc.contributor.authorJ M Jeon-
dc.contributor.authorY H Cheong-
dc.contributor.authorW S Chung-
dc.contributor.authorC O Lim-
dc.contributor.authorJ Y Kim-
dc.contributor.authorByung Dae Yoon-
dc.contributor.authorS Y Lee-
dc.contributor.authorCha Young Kim-
dc.date.accessioned2017-04-19T09:27:23Z-
dc.date.available2017-04-19T09:27:23Z-
dc.date.issued2011-
dc.identifier.issn0304-4165-
dc.identifier.uri10.1016/j.bbagen.2011.06.021ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10472-
dc.description.abstractBackground: The C2 domain is a Ca2+/phospholipid-binding motif found in many proteins involved in signal transduction or membrane trafficking. OsERG3 is a homolog of OsERG1, a gene encoding a small C2-domain protein in rice. Methods: OsERG3 Ca2+-binding and phospholipid-binding assays were carried out using 3H-labeled phospholipid liposomes and a 45Ca2+ overlay assay, respectively. Cytosolic expression of OsERG3 was investigated by Western blot analysis and the OsERG3::smGFP transient expression assay. Results: OsERG3 transcript levels were greatly enhanced by treatment with a fungal elicitor and Ca2+-ionophore. OsERG3 protein proved unable to interact with phospholipids regardless of the presence or absence of Ca2+ ions. Nonetheless, OsERG3 displayed calcium-binding activity in an in vitro45Ca2+-binding assay, a property not observed with OsERG1. The cytosolic location of OsERG3 was not altered by the presence of fungal elicitor or Ca2+-ionophore. Conclusions: OsERG3 encodes a small C2-domain protein consisting of a single C2 domain. OsERG3 binds Ca2+ ions but not phospholipids. OsERG3 is a cytosolic soluble protein. The OsERG3 gene may play a role in signaling pathway involving Ca2+ ions. General significance: The data demonstrate that OsERG3 is an unusual small C2-domain protein containing a Ca2+- binding module but lacking phospholipid-binding properties.-
dc.publisherElsevier-
dc.titleRice OsERG3 encodes an unusual small C2-domain protein containing a Ca2+-binding module but lacking phospholipid-binding properties-
dc.title.alternativeRice OsERG3 encodes an unusual small C2-domain protein containing a Ca2+-binding module but lacking phospholipid-binding properties-
dc.typeArticle-
dc.citation.titleBiochimica et Biophysica Acta-General Subjects-
dc.citation.number12-
dc.citation.endPage1322-
dc.citation.startPage1317-
dc.citation.volume1810-
dc.contributor.affiliatedAuthorByung Dae Yoon-
dc.contributor.affiliatedAuthorCha Young Kim-
dc.contributor.alternativeName강창호-
dc.contributor.alternativeName문병철-
dc.contributor.alternativeName박형철-
dc.contributor.alternativeName구성철-
dc.contributor.alternativeName전주미-
dc.contributor.alternativeName정용화-
dc.contributor.alternativeName정우식-
dc.contributor.alternativeName임채오-
dc.contributor.alternativeName김재연-
dc.contributor.alternativeName윤병대-
dc.contributor.alternativeName이상열-
dc.contributor.alternativeName김차영-
dc.identifier.bibliographicCitationBiochimica et Biophysica Acta-General Subjects, vol. 1810, no. 12, pp. 1317-1322-
dc.identifier.doi10.1016/j.bbagen.2011.06.021-
dc.subject.keywordCa2+/ phospholipid binding-
dc.subject.keywordRice-
dc.subject.keywordSignal transduction-
dc.subject.keywordSmall C2-domain protein-
dc.subject.localCa2+/ phospholipid binding-
dc.subject.localCa2+/phospholipid-binding-
dc.subject.localRice-
dc.subject.localRice (Oryza sativa L)-
dc.subject.localRice (Oryza sativa L.)-
dc.subject.localrice-
dc.subject.localrice (Oryza sativa)-
dc.subject.localOryza sativa-
dc.subject.localOryza sativa L-
dc.subject.localOryza sativa L.-
dc.subject.localoryza sativa-
dc.subject.localsignal transduction-
dc.subject.localSignal transduction-
dc.subject.localSignal trasduction-
dc.subject.localSmall C2-domain protein-
dc.subject.localsmall C2-domain protein-
dc.description.journalClassY-
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Jeonbuk Branch Institute > 1. Journal Articles
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