%0 Journal Article
%T Characterization of metalloprotease of Slr0643 and Sll0862, the S2P homologs from Synechocystis sp. PCC6803<br>集胞藻PCC6803中S2P同源蛋白Slr0643及Sll0862 金属蛋白酶活性的体外鉴定
%A Chunyan Qin
%A Xu Zhang
%A Gu Chen
%A <br>秦春燕
%A 张旭
%A 陈谷
%J 微生物学报
%D 2012
%I 
%X Objective]It is a conserved mechanism in bacteria that metalloprotease site-2 protease(S2P) cleaves transmembrane anti-sigma factor to release sequestered sigma factor in response to extracytoplasmic stress.However,the function of site-2 protease homologs in cyanobacteria remains elusive,so we investigated the metalloprotease activity of Slr0643 and Sll0862,the site-2 protease homologs from Synechocystis sp.PCC6803.Methods] Recombinant Slr0643 and Sll0862 were constructed and overexpressed in Escherichia coli BL21(CE3).Their protease activities were tested against β-casein and then resolved on SDS-PAGE.Results] Results from caseinolytic assay indicated that Slr0643 and Sll0862 have proteolytic activity which is blocked by o-phenanthroline,a metalloprotease inhibitor.These metalloprotease activity of Slr0643 and Sll0862 in vitro provide the foundation for futher analysis of their substrates in vivo.Conclusion] The site-2 protease homologs in Synechocystis sp.PCC6803 have metalloprotease activity.
%K Synechocystis sp
%K PCC6803
%K S2P metalloprotease
%K Slr0643
%K Sll0862
%K prokaryotic expression
%K purification
%K metalloprotease activity assay in vitro<br>集胞藻PCC6803
%K S2P金属蛋白酶
%K Slr0643
%K Sll0862
%K 原核表达
%K 纯化
%K 体外酶活鉴定
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=3B2CD3BB807ED8FA94AA1396C58C25CC&yid=99E9153A83D4CB11&vid=286FB2D22CF8D013&iid=CA4FD0336C81A37A&sid=B47A0E731AF43EB2&eid=5E25104E99903E8A&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=0