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AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana

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Abstract

Plants express many calmodulins (CaMs) and calmodulin-like (CML) proteins that sense and transduce different Ca2+ signals. Previously, we reported divergent soybean (Glycine max) CaM isoforms (GmCaM4/5) with differential abilities to activate CaM-dependent enzymes. To elucidate biological functions of divergent CaM proteins, we isolated a cDNA encoding a CML protein, AtCML8, from Arabidopsis. AtCML8 shows highest identity with GmCaM4 at the protein sequence level. Expression of AtCML8 was high in roots, leaves, and flowers but low in stems. In addition, the expression of AtCML8 was induced by exposure to salicylic acid or NaCl. AtCML8 showed typical characteristics of CaM such as Ca2+-dependent electrophoretic mobility shift and Ca2+ binding ability. In immunoblot analyses, AtCML8 was recognized only by antiserum against GmCaM4 but not by GmCaM1 antibodies. Interestingly, AtCML8 was able to activate phosphodiesterase (PDE) but did not activate NAD kinase. These results suggest that AtCML8 acts as a CML protein in Arabidopsis with characteristics similar to soybean divergent GmCaM4 at the biochemical levels.

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Acknowledgments

We thank Dr. Hans J. Bohnert for critical reading and insightful comments. This work was supported by grants from World Class University Program (R32-10148) funded by MOEST and by BioGreen 21 Program (20080401034023) funded by RDA. KEK was supported by scholarship from the BK21 program of MOEST.

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Correspondence to Hyeong Cheol Park or Woo Sik Chung.

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Communicated by J. R. Liu.

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Park, H.C., Park, C.Y., Koo, S.C. et al. AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana . Plant Cell Rep 29, 1297–1304 (2010). https://doi.org/10.1007/s00299-010-0916-7

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