Protein–Protein Contacts that Activate and Repress Prokaryotic Transcription
Open Access
- 1 March 1998
- Vol. 92 (5) , 597-600
- https://doi.org/10.1016/s0092-8674(00)81126-5
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Transcription Activation or Repression by Phage Φ29 Protein p4 Depends on the Strength of the RNA Polymerase–Promoter InteractionsMolecular Cell, 1997
- Changing the mechanism of transcriptional activation by phage λ repressorProceedings of the National Academy of Sciences, 1997
- Activation of prokaryotic transcription through arbitrary protein–protein contactsNature, 1997
- RNA Polymerase β′ Subunit: A Target of DNA Binding-Independent ActivationScience, 1997
- Transcription Activation by the Bacteriophage Mu Mor Protein Requires the C-terminal Regions of Both α and σ70 Subunits of Escherichia coli RNA PolymerasePublished by Elsevier ,1996
- Crystal Structure of a σ70 Subunit Fragment from E. coli RNA PolymeraseCell, 1996
- DNA-binding determinants of the alpha subunit of RNA polymerase: novel DNA-binding domain architecture.Genes & Development, 1996
- Solution Structure of the Activator Contact Domain of the RNA Polymerase α SubunitScience, 1995
- 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.Proceedings of the National Academy of Sciences, 1995
- Promoter structure, promoter recognition, and transcription activation in prokaryotesCell, 1994