Effects of R100 Mutant MerR on Regulation of mer Operon from Shigella flexneri

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, Cysl17Ser, and Cys126Ser mutations abolished the inducibility of the mer operon and the Hisl18Ala mutation resulted in the reduction of inducibility (about 9.1 % remaining) in complementation experiment in the presence of at subtoxic level (). The complementation experiment with absent showed that Hisl18Ala, Cys126Ser, and wild-type MerR could repress the operon but Cysl17Ser could not, and the amino-terminal deletion mutant could neither induce nor repress the R100 mer operon.