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.
Plant Molecular Biology – Springer Journals
Published: Oct 13, 2004
It’s your single place to instantly
discover and read the research
that matters to you.
Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.
All for just $49/month
Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly
Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.
All the latest content is available, no embargo periods.
“Whoa! It’s like Spotify but for academic articles.”@Phil_Robichaud