Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution (Q27638951)

7

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author name string

Dmitry G Vassylyev

1

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Oleg Laptenko

3

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Jookyung Lee

4

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Marina N Vassylyeva

5

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Sergei Borukhov

Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution

6

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language of work or name

English

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publication date

13 June 2002

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published in

Nature

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volume

417

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page(s)

712-9

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issue

6890

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cites work

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Prokaryotic and eukaryotic RNA polymerases have homologous core subunits

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Factor Stimulating Transcription by RNA Polymerase

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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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sigma factor mutations affecting the sequence-selective interaction of RNA polymerase with -10 region single-stranded DNA

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The interface of sigma with core RNA polymerase is extensive, conserved, and functionally specialized

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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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Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution.

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A structural model of transcription elongation

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Structural organization of the RNA polymerase-promoter open complex

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A mutant Escherichia coli sigma 70 subunit of RNA polymerase with altered promoter specificity

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Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase

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Mutational analysis of beta '260-309, a sigma 70 binding site located on Escherichia coli core RNA polymerase.

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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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Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes.

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Organization of open complexes at Escherichia coli promoters. Location of promoter DNA sites close to region 2.5 of the sigma70 subunit of RNA polymerase

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Mapping the promoter DNA sites proximal to conserved regions of sigma 70 in an Escherichia coli RNA polymerase-lacUV5 open promoter complex

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A "master" in base unpairing during isomerization of a promoter upon RNA polymerase binding.

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Interactions of Escherichia coli sigma(70) within the transcription elongation complex

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Processing of X-ray diffraction data collected in oscillation mode

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Detecting and overcoming crystal twinning

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Raster3D: photorealistic molecular graphics

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Isolation and characterization of sigma(70)-retaining transcription elongation complexes from Escherichia coli

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Characterization of the Escherichia coli transcription factor sigma 70: localization of a region involved in the interaction with core RNA polymerase

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Amino-terminal amino acids modulate sigma-factor DNA-binding activity

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Altered promoter recognition by mutant forms of the sigma 70 subunit of Escherichia coli RNA polymerase

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[22] Detecting and overcoming crystal twinning

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Further additions to MolScript version 1.4, including reading and contouring of electron-density maps

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Identifiers

DOI

10.1038/NATURE752

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

715717

1053504154

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715717

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference