Requirement of calcium binding, myristoylation, and protein-protein interaction for the Copine BON1 function in Arabidopsis.

ABSTRACT: Copines are highly conserved proteins with lipid-binding activities found in animals, plants, and protists. They contain two calcium-dependent phospholipid binding C2 domains at the amino terminus and a VWA domain at the carboxyl terminus. The biological roles of most copines are not understood and the biochemical properties required for their functions are largely unknown. The Arabidopsis copine gene BON1/CPN1 is a negative regulator of cell death and defense responses. Here we probed the potential biochemical activities of BON1 through mutagenic studies. We found that mutations of aspartates in the C2 domains did not alter plasma membrane localization but compromised BON1 activity. Mutation at putative myristoylation residue glycine 2 altered plasma membrane localization of BON1 and rend

SUBMITTER: Li Y 

PROVIDER: S-EPMC2943284 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature