Probing the assembly of transcription initiation complexes through changes in sigmaN protease sensitivity. - Wikidata - wikimedia - TriplyDB

Probing the assembly of transcription initiation complexes through changes in sigmaN protease sensitivity.

Probing the assembly of transcription initiation complexes through changes in sigmaN protease sensitivity.

http://www.wikidata.org/entity/Q36638290

about

Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action Construction and functional analyses of a comprehensive sigma54 site-directed mutant library using alanine-cysteine mutagenesis The bacterial enhancer-dependent sigma(54) (sigma(N)) transcription factor Functionality of purified sigma(N) (sigma(54)) and a NifA-like protein from the hyperthermophile Aquifex aeolicus.In vitro roles of invariant helix-turn-helix motif residue R383 in sigma(54) (sigma(N)).The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54.Promoter opening by sigma(54) and sigma(70) RNA polymerases: sigma factor-directed alterations in the mechanism and tightness of control Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes.Correlating protein footprinting with mutational analysis in the bacterial transcription factor sigma54 (sigmaN).The role of region II in the RNA polymerase sigma factor sigma(N) (sigma(54)).Identification of an N-terminal region of sigma 54 required for enhancer responsiveness Single amino acid substitution mutants of Klebsiella pneumoniae sigma(54) defective in transcription.Amino-terminal sequences of sigmaN (sigma54) inhibit RNA polymerase isomerization.A common feature from different subunits of a homomeric AAA+ protein contacts three spatially distinct transcription elements.Interaction of sigma factor sigmaN with Escherichia coli RNA polymerase core enzyme Mapping sigma 54-RNA polymerase interactions at the -24 consensus promoter element.A role for the conserved GAFTGA motif of AAA+ transcription activators in sensing promoter DNA conformation.The interaction between sigmaS, the stationary phase sigma factor, and the core enzyme of Escherichia coli RNA polymerase.New roles for conserved regions within a sigma 54-dependent enhancer-binding protein.Activation and repression of transcription by differential contact: two sides of a coin.Sequences within the DNA cross-linking patch of sigma 54 involved in promoter recognition, sigma isomerization, and open complex formation.Low Resolution Structure of the ς54 Transcription Factor Revealed by X-ray Solution Scattering

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P2860

Probing the assembly of transcription initiation complexes through changes in sigmaN protease sensitivity.

http://www.wikidata.org/entity/Q36638290

description

1997 nî lūn-bûn

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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1997年论文

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name

Probing the assembly of transc ...... n sigmaN protease sensitivity.

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Probing the assembly of transc ...... n sigmaN protease sensitivity.

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Probing the assembly of transc ...... n sigmaN protease sensitivity.

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Probing the assembly of transc ...... n sigmaN protease sensitivity.

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Probing the assembly of transc ...... n sigmaN protease sensitivity.

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Probing the assembly of transc ...... n sigmaN protease sensitivity.

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PNAS.94.22.12145

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Proceedings of the National Academy of Sciences of the United States of America

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Probing the assembly of transc ...... n sigmaN protease sensitivity.

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Buck M

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Casaz P

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P2860

The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

Binding of the sigma 70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting.

Probing the Escherichia coli glnALG upstream activation mechanism in vivo

DNA-looping and enhancer activity: association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter

Protein crosslinking studies suggest that Rhizobium meliloti C4-dicarboxylic acid transport protein D, a sigma 54-dependent transcriptional activator, interacts with sigma 54 and the beta subunit of RNA polymerase.

Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli.

Protease footprinting reveals a surface on transcription factor TFIIB that serves as an interface for activators and coactivators

Specific binding of the transcription factor sigma-54 to promoter DNA.

RNA polymerase binding using a strongly acidic hydrophobic-repeat region of sigma 54

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12145-12150

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scholarly article

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10.1073/PNAS.94.22.12145

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94

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1997-10-01T00:00:00Z

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13886723

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9342377

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23731

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