Researchers from Gyeongsang National University Provide Details of New Studies and Findings in the Area of Phosphotransferases (Alcohol Group Acceptor)
By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Enzymes and Coenzymes. According to news reporting originating in Jinju, South Korea, by NewsRx journalists, research stated, "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."
The news reporters obtained a quote from the research from Gyeongsang National University, "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. Mutation of Ser41 to alanine (OsERG1S41A) and aspartate (OsERG1S41D) abolishes the ability of OsERG1 to bind phospholipids regardless of the presence or absence of Ca(2+) ions. In addition, unlike the OsERG1 wild-type form, the mutant OsERG1 (S41A)::smGFP construct lost the ability to translocate from the cytosol to the plasma membrane in response to calcium ions or fungal elicitor."
According to the news reporters, the research concluded: "These results indicate that Ser41 may be essential for the function of OsERG1."
For more information on this research see: Rice small C2-domain proteins are phosphorylated by calcium-dependent protein kinase. Molecules and Cells, 2013;35(5):381-7. (Springer - www.springer.com; Molecules and Cells - www.springerlink.com/content/1016-8478/)
Our news correspondents report that additional information may be obtained by contacting C.H. Kang, Division of Applied Life Sciences (Brain Korea 21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, 660-701, South Korea. Additional authors for this research include B.C. Moon, H.C. Park, S.C. Koo, Y.H. Chi, Y.H. Cheong, B.D. Yoon, S.Y. Lee and C.Y Kim (see also Enzymes and Coenzymes).
Keywords for this news article include: Asia, Jinju, Peptides, South Korea, Amino Acids, Protein Kinases, Enzymes and Coenzymes, Phosphotransferases (Alcohol Group Acceptor).
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