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• W2019366453 startingPage "2634" @default.
• W2019366453 abstract "ABSTRACT RNA polymerase of Escherichia coli is the sole enzyme responsible for mRNA synthesis in the cell. Upon binding of a sigma factor, the holoenzyme can direct transcription from specific promoter sequences. We have previously defined a region of the β′ subunit (β′260-309, amino acids 260 to 309) which adopts a coiled-coil conformation shown to interact with σ 70 both in vitro and in vivo. However, it was not known if the coiled-coil conformation was maintained upon binding to σ 70 . In this work, we engineered a disulfide bond within β′240-309 that locks the β′ coiled-coil region in the coiled-coil conformation, and we show that this “locked” peptide is able to bind to σ 70 . We also show that the locked coiled-coil is capable of inducing a conformational change within σ 70 that allows recognition of the −10 nontemplate strand of DNA. This suggests that the coiled-coil does not adopt a new conformation upon binding σ 70 or upon recognition of the −10 nontemplate strand of DNA." @default.
• W2019366453 created "2016-06-24" @default.
• W2019366453 creator A5011520100 @default.
• W2019366453 creator A5058731950 @default.
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• W2019366453 date "2002-05-15" @default.
• W2019366453 modified "2023-09-24" @default.
• W2019366453 title "Using Disulfide Bond Engineering To Study Conformational Changes in the β′260-309 Coiled-Coil Region of <i>Escherichia coli</i> RNA Polymerase during σ ⁷⁰ Binding" @default.
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• W2019366453 doi "https://doi.org/10.1128/jb.184.10.2634-2641.2002" @default.
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