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

The 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...

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Bibliographic Details
Published in:Science China. Chemistry 2012, Vol.55 (1), p.106-111
Main Authors: Chen, Xing, Hao, ZiYang, Chen, Peng R.
Format: Article
Language:English
Subjects:
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Dimers
E coli
MAR
Photolysis
Proteins
R蛋白
二聚体
体形
大肠杆菌细胞
抗生素耐药性
蛋白质
调节蛋白
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Summary:The 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.
ISSN:1674-7291
1869-1870
DOI:10.1007/s11426-011-4437-1