Protein photocrosslinking reveals dimer of dimers formation on MarR protein in Escherichia coli  

作　　者：CHEN Xing HAO ZiYang CHEN Peng R. 

机构地区：[1]Beijing National Laboratory for Molecular Sciences(BNLMS),Department of Chemical Biology,College of Chemistry and Molecular Engineering,Peking University,Beijing 100871,China

出　　处：《中国科学：化学》2012年第2期223-225,共3页SCIENTIA SINICA Chimica

摘　　要：he multiple antibiotic resistance regulatory protein(MarR) binds to two promoter sites on the marO operator in Escherichia coli.Our study showed that more than one MarR dimer proteins bound to either of its two promoter sites(Site I and Site II),suggesting that MarR might form higher complexes than homodimers when bound to DNA inside E.coli cells.To further verify this hypothesis,we site-specifically incorporated a photocrosslinking probe at the interface between two MarR dimer proteins.Photolysis in living E.coli cells revealed a covalent linkage between the two interdimer subunits of MarR,suggesting that MarR forms dimer of dimers in vivo.he multiple antibiotic resistance regulatory protein（MarR） binds to two promoter sites on the marO operator in Escherichia coli.Our study showed that more than one MarR dimer proteins bound to either of its two promoter sites（Site I and Site II）,suggesting that MarR might form higher complexes than homodimers when bound to DNA inside E.coli cells.To further verify this hypothesis,we site-specifically incorporated a photocrosslinking probe at the interface between two MarR dimer proteins.Photolysis in living E.coli cells revealed a covalent linkage between the two interdimer subunits of MarR,suggesting that MarR forms dimer of dimers in vivo.

关 键 词：大肠杆菌细胞 二聚体 R蛋白 蛋白质 体形 MAR 抗生素耐药性 调节蛋白 

分 类 号：Q936[生物学—微生物学]