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- W2143313672 abstract "The transcription activator protein NtrC (nitrogen regulatory protein C, also termed NR(I)) can catalyze the transition of Escherichia coli RNA polymerase complexed with the sigma(54) factor (RNAP x sigma(54)) from the closed complex (RNAP x sigma(54) bound at the promoter) to the open complex (melting of the promoter DNA). This process involves phosphorylation of NtrC (NtrC-P), assembly of an octameric NtrC-P complex at the enhancer DNA sequence, interaction of this complex with promoter-bound RNAP x sigma(54) via DNA looping, and hydrolysis of ATP. Here it is demonstrated by two-color fluorescence cross-correlation spectroscopy measurements of 6-carboxyfluorescein and 6-carboxy-X-rhodamine-labeled DNA oligonucleotide duplexes that the NtrC-P complex can bind two DNA duplexes simultaneously. This suggests a model for the conformation of the looped intermediate that is formed between NtrC-P and RNAP. sigma(54) at the glnAp2 promoter during the activation process." @default.
- W2143313672 created "2016-06-24" @default.
- W2143313672 creator A5063410783 @default.
- W2143313672 date "2000-02-29" @default.
- W2143313672 modified "2023-09-27" @default.
- W2143313672 title "Simultaneous Binding of Two DNA Duplexes to the NtrC−Enhancer Complex Studied by Two-Color Fluorescence Cross-Correlation Spectroscopy" @default.
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- W2143313672 doi "https://doi.org/10.1021/bi9922190" @default.
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