The subcellular localization of an unusual rice calmodulin isoform, OsCaM61, depends on its prenylation status.
Plant Mol Biol
; 48(3): 203-10, 2002 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-11855722
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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oryza
/
Calmodulina
Idioma:
En
Revista:
Plant Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
/
BOTANICA
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
China