Kinetic Studies and Structural Models of the Association of E.coli σ70 RNA Polymerase with the λPR Promoter: Large Scale Conformational Changes in Forming the Kinetically Significant Intermediates
- 30 May 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 319 (3) , 649-671
- https://doi.org/10.1016/s0022-2836(02)00293-0
Abstract
No abstract availableKeywords
This publication has 105 references indexed in Scilit:
- Differential melting of the transcription start site associated with changes in RNA polymerase-promoter contacts in initiating transcription complexesJournal of Molecular Biology, 2001
- RNA Polymerase: Structural Similarities Between Bacterial RNA Polymerase and Eukaryotic RNA Polymerase IIJournal of Molecular Biology, 2000
- The Protein Data BankNucleic Acids Research, 2000
- Two conformations of RNA polymerase II revealed by electron crystallographyJournal of Molecular Biology, 1997
- Thermodynamics of the interactions of Lac repressor with variants of the symmetric Lac operator: effects of converting a consensus site to a non-specific siteJournal of Molecular Biology, 1997
- A Zinc-binding Region in the β′ Subunit of RNA Polymerase is Involved in Antitermination of Early Transcription of Phage HK022Journal of Molecular Biology, 1995
- The Thumbs's Knuckle: Flexibility in the Thumb Subdomain of T7 RNA Polymerase is Revealed by the Structure of a T7/T3 RNA PolymeraseJournal of Molecular Biology, 1994
- Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfoldingJournal of Molecular Biology, 1992
- Kinetics of open complex formation between Escherichia coli RNA polymerase and the lac UV5 promoter. Evidence for a sequential mechanism involving three stepsBiochemistry, 1985
- Kinetics and mechanism of the interaction of Escherichia coli RNA polymerase with the λPR promoterJournal of Molecular Biology, 1984