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Andrey Feklistov
Researcher at Rockefeller University
Publications - 16
Citations - 1292
Andrey Feklistov is an academic researcher from Rockefeller University. The author has contributed to research in topics: RNA polymerase & Polymerase. The author has an hindex of 11, co-authored 16 publications receiving 1116 citations. Previous affiliations of Andrey Feklistov include Russian Academy of Sciences & Moscow State University.
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Journal ArticleDOI
Bacterial Sigma Factors: A Historical, Structural, and Genomic Perspective
TL;DR: The key advances in σ biology are recounted, from their discovery 45 years ago to the most recent progress in understanding their structure and function at the atomic level, and both the housekeeping and alternative σs are discussed.
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Structural Basis for Promoter −10 Element Recognition by the Bacterial RNA Polymerase σ Subunit
Andrey Feklistov,Seth A. Darst +1 more
TL;DR: The key step in bacterial promoter opening is recognition of the -10 promoter element (T(-12)A(-11)T(-10),A(-9)A (-8)T (-7) consensus sequence) by the RNA polymerase σ subunit.
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Structure of a bacterial RNA polymerase holoenzyme open promoter complex
TL;DR: In this paper, the authors determined crystal structures, refined to 4.14 A-resolution, of RPo containing Thermus aquaticus RNAP holoenzyme and promoter DNA that includes the full transcription bubble.
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A basal promoter element recognized by free RNA polymerase σ subunit determines promoter recognition by RNA polymerase holoenzyme
Andrey Feklistov,Nataliya Barinova,Anastasiya Sevostyanova,Ewa Heyduk,I. A. Bass,Irina O. Vvedenskaya,Konstantin Kuznedelov,Egle˙ Merkiene˙,Elena Stavrovskaya,Saulius Klimašauskas,Vadim Nikiforov,Tomasz Heyduk,Konstantin Severinov,Andrey Kulbachinskiy +13 more
TL;DR: During transcription initiation by bacterial RNA polymerase, the sigma subunit recognizes the -35 and -10 promoter elements; free sigma, however, does not bind DNA; recognition of bacterial promoters is controlled by independent interactions of sigma with multiple basal promoter elements.
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Rifamycins do not function by allosteric modulation of binding of Mg2+ to the RNA polymerase active center
Andrey Feklistov,Vladimir Mekler,Qiaorong Jiang,Lars F. Westblade,Herbert Irschik,Rolf Jansen,Arkady Mustaev,Seth A. Darst,Richard H. Ebright +8 more
TL;DR: It is shown that rifamycins do not affect the affinity of binding of Mg2+ to the RNAP active center, and the three lines of biochemical evidence are reassessed, obtaining results not supportive of the proposal.