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- W2147060384 abstract "The Escherichia coli gcvTHP operon is under control of the LysR-type transcriptional regulator GcvA. GcvA activates the operon in the presence of glycine and represses the operon in its absence. Repression by GcvA is dependent on a second regulatory protein, GcvR. Generally, LysR-type transcriptional regulators bind to specific small co-effector molecules which results in either their altered affinity for specific binding sites on the DNA or altered ability to bend the DNA, resulting in either activation or repression of their respective operons. This study shows that glycine, the co-activator for the gcv operon, does not alter either GcvA's ability to bind DNA nor its ability to bend DNA. Rather, glycine binds to GcvR, disrupting a GcvA/GcvR interaction required for repression and allowing GcvA activation of the gcvTHP operon. Amino acid changes in GcvR that reduce glycine binding result in a loss of glycine-mediated activation in vivo." @default.
- W2147060384 created "2016-06-24" @default.
- W2147060384 creator A5051036675 @default.
- W2147060384 creator A5053710171 @default.
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- W2147060384 date "2002-07-01" @default.
- W2147060384 modified "2023-09-30" @default.
- W2147060384 title "Glycine binds the transcriptional accessory protein GcvR to disrupt a GcvA/GcvR interaction and allow GcvA-mediated activation of the Escherichia coli gcvTHP operon" @default.
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- W2147060384 doi "https://doi.org/10.1099/00221287-148-7-2203" @default.
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