The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex.
about
Termination and antitermination: RNA polymerase runs a stop signThe Spt4-Spt5 complex: a multi-faceted regulator of transcription elongationStructural basis for the bacterial transcription-repair coupling factor/RNA polymerase interactionArchitecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivityUbiquitous transcription factors display structural plasticity and diverse functions: NusG proteins - Shifting shapes and paradigmsInterdomain contacts control folding of transcription factor RfaH.RNA polymerase elongation factorsFunctional analysis of Thermus thermophilus transcription factor NusGNusG-Spt5 proteins-Universal tools for transcription modification and communication.Post-initiation control by the initiation factor sigmaThe β subunit gate loop is required for RNA polymerase modification by RfaH and NusG.The initiation factor TFE and the elongation factor Spt4/5 compete for the RNAP clamp during transcription initiation and elongationBacterial RNA polymerase can retain σ70 throughout transcription.A novel phage-encoded transcription antiterminator acts by suppressing bacterial RNA polymerase pausingThe primary σ factor in Escherichia coli can access the transcription elongation complex from solution in vivo.Nascent RNA length dictates opposing effects of NusA on antitermination.Functional specialization of transcription elongation factorsA single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its co-regulator KorB.Macromolecular micromovements: how RNA polymerase translocates.Elongation by RNA polymerase: a race through roadblocks.Pause, play, repeat: CDKs push RNAP II's buttons.Single-molecule studies of RNA polymerase: one singular sensation, every little step it takes.A nexus for gene expression-molecular mechanisms of Spt5 and NusG in the three domains of life.Archaeology of RNA polymerase: factor swapping during the transcription cycle.Structural transitions in the transcription elongation complexes of bacterial RNA polymerase during σ-dependent pausing.A global analysis of transcription reveals two modes of Spt4/5 recruitment to archaeal RNA polymerase.σ38-dependent promoter-proximal pausing by bacterial RNA polymeraseFunctional regions of the N-terminal domain of the antiterminator RfaH.E. coli NusG inhibits backtracking and accelerates pause-free transcription by promoting forward translocation of RNA polymeraseInitial transcribed region sequences influence the composition and functional properties of the bacterial elongation complex.High-mobility-group a-like CarD binds to a DNA site optimized for affinity and position and to RNA polymerase to regulate a light-inducible promoter in Myxococcus xanthus.Nano positioning system reveals the course of upstream and nontemplate DNA within the RNA polymerase II elongation complex.Looking for a promoter in 3D.Structure and Function of RNA Polymerases and the Transcription Machineries.Reading of the non-template DNA by transcription elongation factors.The universally-conserved transcription factor RfaH is recruited to a hairpin structure of the non-template DNA strand.Transcriptional control of RfaH on polysialic and colanic acid synthesis by Escherichia coli K92.Mutations in β' subunit of Escherichia coli RNA polymerase perturb the activator polymerase functional interaction required for promoter clearance.Domain interactions of the transcription-translation coupling factor Escherichia coli NusG are intermolecular and transient.
P2860
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P2860
The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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name
The elongation factor RfaH and ...... nscription elongation complex.
@ast
The elongation factor RfaH and ...... nscription elongation complex.
@en
type
label
The elongation factor RfaH and ...... nscription elongation complex.
@ast
The elongation factor RfaH and ...... nscription elongation complex.
@en
prefLabel
The elongation factor RfaH and ...... nscription elongation complex.
@ast
The elongation factor RfaH and ...... nscription elongation complex.
@en
P2093
P2860
P356
P1476
The elongation factor RfaH and ...... nscription elongation complex.
@en
P2093
Anastasiya Sevostyanova
Dmitry G Vassylyev
Vladimir Svetlov
P2860
P304
P356
10.1073/PNAS.0708432105
P407
P577
2008-01-14T00:00:00Z