Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 17, Pages 5954-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja101663d
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Funding
- Wellcome Trust [079351/Z/06/Z]
- BBSRC [BB/E008232/1]
- DFG [SFB 431 P18]
- Wellcome Trust [079351/Z/06/Z] Funding Source: Wellcome Trust
- BBSRC [BB/E008232/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E008232/1] Funding Source: researchfish
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RNA polymerases (RNAP) carry out transcription, the first step in the highly regulated process of gene expression. RNAPs are complex multisubunit enzymes, which undergo extensive structural rearrangements during the transcription cycle (initiation-elongation-termination). They accommodate interactions with the nucleic acid scaffold of transcription complexes (template DNA, DNA/RNA hybrid, and nascent RNA) and interact with a plethora of transcription factors. Here we focused on the RNAP-F/E subcomplex, which forms a stable heterodimer that binds the nascent RNA and thereby stimulates the processivity of elongation complexes. We used the pulsed-EPR method DEER and fluorescence spectroscopy to probe for conformational changes within the F/E dimer. Our results demonstrate that, upon binding of RNA, F/E remains in a stable conformation, which suggests that it serves as a structurally rigid guiding rail for the growing RNA chain during transcription.
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