Activity Determination of 4 Glycosyltransferases and Protein Interaction Analysis of Erwinia beijingensis
Erwinia beijingensis can cause the bacterial soft rot disease of Pleurotus eryngii.In order to clarify the function of glycosyltransferase in E.beijingensis,a recombinant expression vector was constructed to express and purify the glycosyltransferase in this pathogen.The protein activity was measured,and the interactions between proteins were analyzed.The results showed that the prokaryotic expression vector was successfully constructed,4 soluble proteins were obtained,and MshA,WbnH2,EpsH and TuaG proteins were purified by affinity chromatography column.The activity assay showed that four proteins preferentially used UDP galactose.GST pull down results confirmed that WbnH2 and TuaG proteins interacted with MshA and EpsH proteins in vitro,respectively.Above results laid a foundation for the subsequent study on the function of the glycosyltransferase gene in E.beijingensis.
国家科技期刊平台
NSTL
万方数据
维普
