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DC Field | Value | Language |
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dc.citation.endPage | 19314 | - |
dc.citation.number | 22 | - |
dc.citation.startPage | 19304 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 277 | - |
dc.contributor.author | Kim, MC | - |
dc.contributor.author | Lee, SH | - |
dc.contributor.author | Kim, JK | - |
dc.contributor.author | Chun, HJ | - |
dc.contributor.author | Choi, MS | - |
dc.contributor.author | Chung, WS | - |
dc.contributor.author | Moon, BC | - |
dc.contributor.author | Kang, CH | - |
dc.contributor.author | Park, Chan Young | - |
dc.contributor.author | Yoo, JH | - |
dc.contributor.author | Kang, YH | - |
dc.contributor.author | Koo, SC | - |
dc.contributor.author | Koo, YD | - |
dc.contributor.author | Jung, JC | - |
dc.contributor.author | Kim, ST | - |
dc.contributor.author | Schulze-Lefert, P | - |
dc.contributor.author | Lee, SY | - |
dc.contributor.author | Cho, Moo Je | - |
dc.date.accessioned | 2023-12-22T11:38:24Z | - |
dc.date.available | 2023-12-22T11:38:24Z | - |
dc.date.created | 2014-09-23 | - |
dc.date.issued | 2002-05 | - |
dc.description.abstract | Transient influx of Ca2+ constitutes an early event in the signaling cascades that trigger plant defense responses. However, the downstream components of defense-associated Ca2+ signaling are largely unknown. Because Ca2+ signals are mediated by Ca2+-binding proteins, including calmodulin (CaM), identification and characterization of CaM-binding proteins elicited by pathogens should provide insights into the mechanism by which Ca2+ regulates defense responses. In this study, we isolated a gene encoding rice Mlo (Oryza sativa Mlo; OsMlo) using a protein-protein interaction-based screening of a cDNA expression library constructed from pathogen-elicited rice suspension cells. OsMlo has a molecular mass of 62 kDa and shares 65% sequence identity and scaffold topology with barley Mlo, a heptahelical transmembrane protein known to function as a negative regulator of broad spectrum disease resistance and leaf cell death. By using gel overlay assays, we showed that OsMlo produced in Escherichia coli binds to soybean CaM isoform-1 (SCaM-1) in a Ca2+-dependent manner. We located a 20-amino acid CaM-binding domain (CaMBD) in the OsMlo C-terminal cytoplasmic tail that is necessary and sufficient for Ca2+-dependent CaM complex formation. Specific binding of the conserved CaMBD to CaM was corroborated by site-directed mutagenesis, a gel mobility shift assay, and a competition assay with a Ca2+/CaM-dependent enzyme. Expression of OsMlo was strongly induced by a fungal pathogen and by plant defense signaling molecules. We propose that binding of Ca2+-loaded CaM to the C-terminal tail may be a common feature of Mlo proteins. | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.22, pp.19304 - 19314 | - |
dc.identifier.doi | 10.1074/jbc.M108478200 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-0037205430 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/6284 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037205430 | - |
dc.identifier.wosid | 000175894800010 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein - Isolation and characterization of a rice Mlo homologue | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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