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- W2162565066 endingPage "1714" @default.
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- W2162565066 abstract "RNA polymerase core enzyme of Escherichia coli is composed of two α subunits and one each of the β and β′ subunits. The C-terminal domain of the RNA polymerase α subunit plays a key role in molecular communications with class I transcription factors and upstream (UP) elements of promoter DNA, using the same protein surface. To identify possible differences in the functional roles of the two α subunits, we have developed a reconstitution method for hybrid RNA polymerases containing two distinct α subunit derivatives in a defined orientation (“oriented α-heterodimer”). The binding sites of two α C-terminal domains on the UP element DNA were determined by hydroxyl radical-based DNA cleavage mediated by ( p -bromoacetamidobenzyl)-EDTA·Fe, which was bound at Cys-269 on the UP recognition surface of one or both α subunits. The results clearly indicated that the two α subunits bind in tandem to two helix turns of the rrnB P1 UP element, and that the β′-associated α subunit is bound to the promoter–distal region." @default.
- W2162565066 created "2016-06-24" @default.
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- W2162565066 date "1997-03-04" @default.
- W2162565066 modified "2023-09-23" @default.
- W2162565066 title "The two α subunits of <i>Escherichia coli</i> RNA polymerase are asymmetrically arranged and contact different halves of the DNA upstream element" @default.
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- W2162565066 doi "https://doi.org/10.1073/pnas.94.5.1709" @default.
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