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KMID : 0545119940040040245
Journal of Microbiology and Biotechnology
1994 Volume.4 No. 4 p.245 ~ p.249
Effects of R100 Mutant MerR on Regulation of mer Operon from Shigella flexneri
Yoon Kyung-Pyo
Abstract
An amino-terminal 14 amino acids deletion and three site-directed mutations were created to investigate the mechanism of induction and repression of MerR regulatory protein in R100 mer operon from gramnegative Shigella flexneri. The amino-terminal 14 amino acids deletion,Cys117Ser, and Cys126Ser mutations abolished the inducibility of the mer operon and the His118Ala mutation resulted in the reduction of inducibility (about 9.1% remaining) in complementation experiment in the presence of Hg^2+ at subtoxic level (1¥ìM). The complementation experiment with Hg^2+ absent showed that His118Ala, Cys126Ser, and wild-type MerR could repress the operon but Cys117Ser could not, and the amino-terminal deletion mutant could neither induce nor repress the R100 mer operon.
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