%0 Journal Article
%T Phosphoproteomic investigation of Clostridium acetobutylicum<br>丙酮丁醇梭菌磷酸化蛋白质组分析
%A Xue Bai
%A Jingjing Zhao
%A Qian Wang
%A Wei Tong
%A Jiyuan Zhang
%A Jin Zi
%A Zhen Chen
%A Siqi Liu
%A Quanhui Wang
%A <br>白雪
%A 赵晶晶
%A 王倩
%A 童维
%A 张继远
%A 訾金
%A 陈真
%A 刘斯奇
%A 王全会
%J 生物工程学报
%D 2010
%I 
%X Protein phosphorylation in bacteria is important for signaling and metabolic activity. Clostridium acetobutyicum can synthesize high yield of organic solvent under acidic condition. How solventogenesis is regulated at molecular level in this bacterium, is not clearly elucidated yet. We used two dimensional electrophoresis (2-DE) and mass spectrometry to have a differential analysis of the bacterial proteins from Clostridium acetobutylicum at acedogenic and solventogenic stage. We focused on these iso-spots with similar molecular mass and different pI values. Totally, eight string spots were identified, which displayed significant changes of pI values as well as spot volumes in response to solventogenic development. The data acquired from mass spectrometry demonstrated that all of the iso-spots contained the phosphrylated peptides. Bioinformatic analysis revealed that these proteins partake in the pathways of solvent synthesis.
%K Clostridium acetobutylicum
%K 2-dementional electrophoresis (2-DE)
%K protein phosphorylation<br>丙酮丁醇梭菌，双向电泳，磷酸化蛋白质组学
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=103B1FAA04ED0C147E2EFBAA02E42FBE&yid=140ECF96957D60B2&vid=96C778EE049EE47D&iid=F3090AE9B60B7ED1&sid=A621DEC64CBC4DA1&eid=6300C37F864D5DEA&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=0