Structural Basis for DNA-Hairpin Promoter Recognition by the Bacteriophage N4 Virion RNA Polymerase
- 1 December 2008
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 32 (5) , 707-717
- https://doi.org/10.1016/j.molcel.2008.11.010
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (AI12575)
This publication has 33 references indexed in Scilit:
- X-ray crystal structure of the polymerase domain of the bacteriophage N4 virion RNA polymeraseProceedings of the National Academy of Sciences, 2008
- Insight into DNA and Protein Transport in Double-Stranded DNA Viruses: The Structure of Bacteriophage N4Journal of Molecular Biology, 2008
- Bacteriophage N4 virion RNA polymerase interaction with its promoter DNA hairpinProceedings of the National Academy of Sciences, 2007
- Phage N4 RNA polymerase II recruitment to DNA by a single-stranded DNA-binding proteinGenes & Development, 2003
- The intercalating β-hairpin of T7 RNA polymerase plays a role in promoter DNA melting and in stabilizing the melted DNA for efficient RNA synthesisJournal of Molecular Biology, 2002
- Regions of the Escherichia coli primary sigma factor σ70 that are involved in interaction with RNA polymerase core enzymeGenes to Cells, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Escherichia coli single-stranded DNA-binding protein is a supercoiled template-dependent transcriptional activator of N4 virion RNA polymerase.Genes & Development, 1992
- Specific sequences and a hairpin structure in the template strand are required for N4 virion RNA polymerase promoter recognitionCell, 1992
- N4 virion RNA polymerase sites of transcription initiationCell, 1985