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RNA polymerase holoenzyme: structure, function and biological implications
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scholarly article
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Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
review article
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Europe PubMed Central
title
RNA polymerase holoenzyme: structure, function and biological implications
(English)
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stated in
Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
author
Evgeny Nudler
series ordinal
2
object named as
Evgeny Nudler
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author name string
Sergei Borukhov
series ordinal
1
1 reference
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Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
publication date
1 April 2003
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Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
published in
Current Opinion in Microbiology
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stated in
Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
volume
6
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Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
page(s)
93-100
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stated in
Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
issue
2
1 reference
stated in
Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
cites work
Prokaryotic and eukaryotic RNA polymerases have homologous core subunits
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RNA polymerase: structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II.
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Bacterial RNA polymerase
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Factor Stimulating Transcription by RNA Polymerase
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The functional and regulatory roles of sigma factors in transcription
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An integrated model of the transcription complex in elongation, termination, and editing.
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DNA footprints of the two kinetically significant intermediates in formation of an RNA polymerase-promoter open complex: evidence that interactions with start site and downstream DNA induce sequential conformational changes in polymerase and DNA.
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The sigma 70 family: sequence conservation and evolutionary relationships
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Eubacterial sigma-factors
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Functional modulation of Escherichia coli RNA polymerase
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The Minimal Gene Complement of Mycoplasma genitalium
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Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)
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Competition among seven Escherichia coli sigma subunits: relative binding affinities to the core RNA polymerase
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Region 2.5 of the Escherichia coli RNA polymerase sigma70 subunit is responsible for the recognition of the 'extended-10' motif at promoters
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Polypeptides containing highly conserved regions of transcription initiation factor σ70 exhibit specificity of binding to promoter DNA
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Promoter recognition and discrimination by EsigmaS RNA polymerase
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Different roles for basic and aromatic amino acids in conserved region 2 of Escherichia coli sigma(70) in the nucleation and maintenance of the single-stranded DNA bubble in open RNA polymerase-promoter complexes
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Base-specific recognition of the nontemplate strand of promoter DNA by E. coli RNA polymerase
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sigma factor mutations affecting the sequence-selective interaction of RNA polymerase with -10 region single-stranded DNA
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Promoter recognition as measured by binding of polymerase to nontemplate strand oligonucleotide
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Escherichia coli promoter opening and -10 recognition: mutational analysis of sigma70.
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Multiple regions on the Escherichia coli heat shock transcription factor sigma32 determine core RNA polymerase binding specificity
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Mapping the sigma70 subunit contact sites on Escherichia coli RNA polymerase with a sigma70-conjugated chemical protease
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The interface of sigma with core RNA polymerase is extensive, conserved, and functionally specialized
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Binding of the initiation factor sigma(70) to core RNA polymerase is a multistep process
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Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution.
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Structural mechanism for rifampicin inhibition of bacterial rna polymerase
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Structure of the bacterial RNA polymerase promoter specificity sigma subunit
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Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex
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Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution
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Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
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Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution
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Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution
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Structural basis of transcription activation: the CAP-alpha CTD-DNA complex
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A structural model of transcription elongation
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The orientation of DNA in an archaeal transcription initiation complex
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Structural organization of the RNA polymerase-promoter open complex
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7 January 2021
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A coiled-coil from the RNA polymerase beta' subunit allosterically induces selective nontemplate strand binding by sigma(70).
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A "master" in base unpairing during isomerization of a promoter upon RNA polymerase binding.
1 reference
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https://api.crossref.org/works/10.1016%2FS1369-5274%2803%2900036-5
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7 January 2021
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Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex
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7 January 2021
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Translocation of sigma(70) with RNA polymerase during transcription: fluorescence resonance energy transfer assay for movement relative to DNA.
1 reference
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Structure-based analysis of RNA polymerase function: the largest subunit's rudder contributes critically to elongation complex stability and is not involved in the maintenance of RNA-DNA hybrid length
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A role for interaction of the RNA polymerase flap domain with the sigma subunit in promoter recognition.
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7 January 2021
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Region 1 of sigma70 is required for efficient isomerization and initiation of transcription by Escherichia coli RNA polymerase
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A mutation in region 1.1 of sigma70 affects promoter DNA binding by Escherichia coli RNA polymerase holoenzyme
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Mapping protein-protein interaction domains using ordered fragment ladder far-western analysis of hexahistidine-tagged fusion proteins
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How sigma docks to RNA polymerase and what sigma does
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Core RNA polymerase from E. coli induces a major change in the domain arrangement of the sigma 70 subunit
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https://api.crossref.org/works/10.1016%2FS1369-5274%2803%2900036-5
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Role of the RNA polymerase sigma subunit in transcription initiation
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Mutational analysis of beta '260-309, a sigma 70 binding site located on Escherichia coli core RNA polymerase.
1 reference
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A single amino acid substitution in sigma E affects its ability to bind core RNA polymerase
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Low concentrations of free hydrophobic amino acids disrupt the Escherichia coli RNA polymerase core-sigma(70) protein-protein interaction
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Identification of the Helicobacter pylori anti-sigma28 factor
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Function of E. coli RNA polymerase sigma factor sigma 70 in promoter-proximal pausing
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Isolation and characterization of sigma(70)-retaining transcription elongation complexes from Escherichia coli
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Identifiers
DOI
10.1016/S1369-5274(03)00036-5
1 reference
stated in
Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
PubMed ID
12732296
1 reference
stated in
Europe PubMed Central
PubMed ID
12732296
retrieved
6 August 2017
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