Plant Molecular Biology

, Volume 48, Issue 3, pp 203–210 | Cite as

The subcellular localization of an unusual rice calmodulin isoform, OsCaM61, depends on its prenylation status

  • Aiwu Dong
  • Hua Xin
  • Yu Yu
  • Chongrong Sun
  • Kaiming Cao
  • Wen-Hui Shen


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.

calmodulin prenylation membrane nucleus isoprenoid 


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Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Aiwu Dong
    • 1
  • Hua Xin
    • 1
  • Yu Yu
    • 1
  • Chongrong Sun
    • 1
  • Kaiming Cao
    • 1
  • Wen-Hui Shen
    • 2
  1. 1.Department of Biochemistry, School of Life SciencesFudan UniversityChina
  2. 2.Institut de Biologie Moléculaire des Plantes du CNRSStrasbourg CédexFrance

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