The subcellular localization of an unusual rice calmodulin isoform,OsCaM61, depends on its prenylation status |
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Authors: | Dong Aiwu Xin Hua Yu Yu Sun Chongrong Cao Kaiming Shen Wen-Hui |
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Institution: | (1) Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, 200433, China;(2) Institut de Biologie Moléculaire des Plantes du CNRS, 12, rue du Général Zimmer, 67084 Strasbourg Cédex, France |
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Abstract: | Calmodulin (CaM) is a small Ca2+-binding protein highly conserved in eukaryotes. We have reported previously a novel rice CaM-like protein (OsCaM61) which contains an N-terminal CaM domain and a C-terminal extension with a potential prenylation site. Here we report in vitro activity assays confirm OsCaM61 as a functional CaM. Using the green fluorescent protein (GFP) as a visual marker, we further studied the subcellular localization of OsCaM61 in stably transformed tobacco cells. The GFP-OsCaM61 fusion protein was membrane-associated whereas OsCaM61-GFP was mainly detected in the nucleoplasm. GFP-OsCaM61 was transported into the nucleoplasm upon a block in isoprenoid biosynthesis by mevinolin treatment of cells. These results indicate that the prenylated OsCaM61 molecules are mainly membrane-associated whereas its unprenylated counterparts are transported into the nucleoplasm. Thus, OsCaM61 may play functions in co-ordinating Ca2+ signaling with isoprenoid metabolism. |
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Keywords: | calmodulin prenylation membrane nucleus isoprenoid |
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