1 2 ChIP - exo interrogation of Crp , DNA , and 3 RNAP holoenzyme interactions 4 5 6

نویسندگان

  • Haythem Latif
  • Stephen Federowicz
  • Ali Ebrahim
  • Janna Tarasova
  • Richard Szubin
  • Jose Utrilla
  • Karsten Zengler
  • Bernhard O. Palsson
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ChIP - exo interrogation of Crp , DNA , and 3 RNAP holoenzyme interactions 4 5 6

21 Numerous in vitro studies have yielded a refined picture of the structural and molecular 22 associations between Cyclic-AMP receptor protein (Crp), the DNA motif, and RNA polymerase 23 (RNAP) holoenzyme. In this study, high-resolution ChIP-exonuclease (ChIP-exo) was applied to 24 study Crp binding in vivo and at genome-scale. Surprisingly, Crp was found to provide little to 25 no protection ...

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Structure of Escherichia coli RNA polymerase holoenzyme at last.

Much of the mechanistic foundations of our knowledge of regulation of gene expression at the transcriptional level have been provided by Escherichia coli and its phages. E. coli RNA polymerase (EcoRNAP) is a multisubunit enzyme composed of a catalytically active core (β′βα2ω); subunits that are evolutionarily related to β′, β, α, and ω are present in DNA-dependent RNAPs of all organisms. In bac...

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Quantitative analysis of the ternary complex of RNA polymerase, cyclic AMP receptor protein and DNA by fluorescence anisotropy measurements.

The in vitro formation of transcription complexes with Escherichia coli RNA polymerase was monitored using fluorescence anisotropy measurements of labeled fragments of DNA. The multicomponent system consisted of holo or core RNA polymerase (RNAP) and lac or gal promoter fragments of DNA (in different configurations), in the presence or absence of CRP activator protein (wt or mutants) with its l...

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Structure of a bacterial RNA polymerase holoenzyme open promoter complex

Initiation of transcription is a primary means for controlling gene expression. In bacteria, the RNA polymerase (RNAP) holoenzyme binds and unwinds promoter DNA, forming the transcription bubble of the open promoter complex (RPo). We have determined crystal structures, refined to 4.14 Å-resolution, of RPo containing Thermus aquaticus RNAP holoenzyme and promoter DNA that includes the full trans...

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A Thermus phage protein inhibits host RNA polymerase by preventing template DNA strand loading during open promoter complex formation

RNA polymerase (RNAP) is a major target of gene regulation. Thermus thermophilus bacteriophage P23-45 encodes two RNAP binding proteins, gp39 and gp76, which shut off host gene transcription while allowing orderly transcription of phage genes. We previously reported the structure of the T. thermophilus RNAP•σA holoenzyme complexed with gp39. Here, we solved the structure of the RNAP•σA holoenzy...

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تاریخ انتشار 2016