Rice small C2-domain proteins are phosphorylated by calcium-dependent protein kinase.

ABSTRACT: We previously reported that OsERG1 and OsERG3 encode rice small C2-domain proteins with different biochemical properties in Ca(2+)- and phospholipid-binding assays. Os-ERG1 exhibited Ca(2+)-dependent phospholipid binding, which was not observed with OsERG3. In the present study, we show that both OsERG1 and OsERG3 proteins exhibit oligomerization properties as determined by native polyacrylamide gel electrophoresis (PAGE) and glutaraldehyde cross-linking experiments. Furthermore, in vitro phosphorylation assays reveal the phosphorylation of OsERG1 and OsERG3 by a rice calcium-dependent protein kinase, OsCDPK5. Our mutation analysis on putative serine phosphorylation sites shows that the first serine (Ser) at position 41 of OsERG1 may be an essential residue for phosphorylation by OsCDPK5.

SUBMITTER: Kang CH 

PROVIDER: S-EPMC3887858 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature