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• W1832355425 endingPage "6418" @default.
• W1832355425 startingPage "6411" @default.
• W1832355425 abstract "ABSTRACT Previously, we have shown that expression of the Escherichia coli aroP P2 promoter is partially repressed by the TyrR protein alone and strongly repressed by the TyrR protein in the presence of the coeffector tyrosine or phenylalanine (P. Wang, J. Yang, and A. J. Pittard, J. Bacteriol. 179:4206–4212, 1997). Here we present in vitro results showing that the TyrR protein and RNA polymerase can bind simultaneously to the aroP P2 promoter. In the presence of tyrosine, the TyrR protein inhibits open complex formation at the P2 promoter, whereas in the absence of any coeffector or in the presence of phenylalanine, the TyrR protein inhibits a step(s) following the formation of open complexes. We also present mutational evidence which implicates the N-terminal domain of the TyrR protein in the repression of P2 expression. The TyrR binding site of aroP , which includes one weak and one strong TyrR box, is located 5 bp downstream of the transcription start site of P2. Results from a mutational analysis show that the strong box (which is located more closely to the P2 promoter), but not the weak box, plays a critical role in P2 repression." @default.
• W1832355425 created "2016-06-24" @default.
• W1832355425 creator A5063355829 @default.
• W1832355425 creator A5073297994 @default.
• W1832355425 creator A5086963474 @default.
• W1832355425 date "1999-10-15" @default.
• W1832355425 modified "2023-10-18" @default.
• W1832355425 title "Mechanism of Repression of the <i>aroP</i> P2 Promoter by the TyrR Protein of <i>Escherichia coli</i>" @default.
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• W1832355425 doi "https://doi.org/10.1128/jb.181.20.6411-6418.1999" @default.
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