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CML 10, a variant of calmodulin, modulates ascorbic acid synthesis
Author(s) -
Cho KwangMoon,
Nguyen Ha Thi Kim,
Kim Soo Youn,
Shin Jin Seok,
Cho Dong Hwa,
Hong Seung Beom,
Shin Jeong Sheop,
Ok Sung Han
Publication year - 2016
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.13612
Subject(s) - ascorbic acid , arabidopsis , mutant , arabidopsis thaliana , calmodulin , biochemistry , microbiology and biotechnology , effector , phenotype , biology , saccharomyces cerevisiae , yeast , protein–protein interaction , chemistry , enzyme , genetics , gene , food science
Summary Calmodulins (CaMs) regulate numerous Ca 2+ ‐mediated cellular processes in plants by interacting with their respective downstream effectors. Due to the limited number of CaMs, other calcium sensors modulate the regulation of Ca 2+ ‐mediated cellular processes that are not managed by CaMs. Of 50 CaM‐like ( CML ) proteins identified in Arabidopsis thaliana , we characterized the function of CML 10. Yeast two‐hybrid screening revealed phosphomannomutase ( PMM ) as a putative interaction partner of CML 10. In vitro and in vivo interaction assays were performed to analyze the interaction mechanisms of CML 10 and PMM . PMM activity and the phenotypes of cml10 knock‐down mutants were studied to elucidate the role(s) of the CML 10– PMM interaction. PMM interacted specifically with CML 10 in the presence of Ca 2+ through its multiple interaction motifs. This interaction promoted the activity of PMM . The phenotypes of cml10 knock‐down mutants were more sensitive to stress conditions than wild‐type plants, corresponding with the fact that PMM is an enzyme which modulates the biosynthesis of ascorbic acid, an antioxidant. The results of this research demonstrate that a calcium sensor, CML 10, which is an evolutionary variant of CaM, modulates the stress responses in Arabidopsis by regulating ascorbic acid production.