Effect Of Acetylation On The Iorn-containing Superoxide Dismutase (SodB) Of Escherichia Coli

Protein modifications were biologically important events. Protein acetylationwas one of important modifications, and involved in all biological activities.It was ahighly regulated inverse process. It can be deacelylated by a NAD+-dependentdeacetylase Sir2. SodB (Fe-SOD) was a kind of SODs and mainly existed inprokaryotes. It can clear the O2and protect the body free from poison. Currently,there were many studies on the SodB, and more depth in researching it, but a fewstudies on its acetylation. A acetylation site exisisted the51ts anmino-Lys of SodBwas identified in the E. coli in2009by Zhao Yingming et al. and a acetylation siteexisisted the44ts anmino-Lys SodB homologous protein was found in the Salmonellain2010by Zhao Shiming et al.also, in addition, there were only a little furtherreported on SodB acetylation.In view of this, we confirmed SodB from E. coli is acetylated by Western blotand mass spectrometry two ways in this study. And a new acetylation site the12ts Lysof SodB protein was found by us. Meanwhele, we found CobB maybe can catalyticSodB deacetylation by Western blot. We also found SodB activity increased afterdeacetylating by CobB, comparing before SodB deacetylating. In order to furtheranalysis SodB acetylation in vivo, a W3110ΔsodB mutantant was constructed by Redrecombination technology by us. It showed that SodB acetylation level in vivoslightly higher in the W3110ΔsodB than in the wild-type by Genetics analysis.Thereby, it indicated the CobB maybe can regulation SodB deacetylation in thecertain extent in vivo.