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Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of [[sigma].sup.70] domain 1.1.(BIOCHEMISTRY)(Report)(Author abstract)

Bae, Brian ; Davis, Elizabeth ; Brown, Daniel ; Campbell, Elizabeth A. ; Wigneshweraraj, Sivaramesh ; Darst, Seth A.

Proceedings of the National Academy of Sciences of the United States, Dec 3, 2013, Vol.110(49), p.19772(6) [Tạp chí có phản biện]

ISSN: 0027-8424

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  • Nhan đề:
    Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of [[sigma].sup.70] domain 1.1.(BIOCHEMISTRY)(Report)(Author abstract)
  • Tác giả: Bae, Brian ; Davis, Elizabeth ; Brown, Daniel ; Campbell, Elizabeth A. ; Wigneshweraraj, Sivaramesh ; Darst, Seth A.
  • Chủ đề: Escherichia Coli -- Physiological Aspects ; Escherichia Coli -- Genetic Aspects ; Rna Polymerases -- Physiological Aspects ; Gene Expression -- Research
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, Dec 3, 2013, Vol.110(49), p.19772(6)
  • Mô tả: Bacteriophage T7 encodes an essential inhibitor of the Escherichia coli host RNA polymerase (RNAP), the product of gene 2 (Gp2). We determined a series of X-ray crystal structures of E. coli RNAP holoenzyme with or without Gp2. The results define the structure and location of the RNAP [[sigma].sup.70] subunit domain 1.1 ([[sigma].sup.70.sub.1.1]) inside the RNAP active site channel, where it must be displaced by the DNA upon formation of the open promoter complex. The structures and associated data, combined with previous results, allow for a complete delineation of the mechanism for Gp2 inhibition of E. coli RNAP. In the primary inhibition mechanism, Gp2 forms a protein-protein interaction with [[sigma].sup.70.sub.1.1], preventing the normal egress of [[sigma].sup.70.sub.1.1] from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, [[sigma].sup.70.sub.1.1]), to inhibit the function of the enzyme. bacteriophage T7 Gp2 | X-ray crystallography | transcription www.pnas.org/cgi/doi/10.1073/pnas.1314576110
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

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