Function of a Bacterial Activator Protein that Binds to Transcriptional Enhancers

• Published in: Science (American Association for the Advancement of Science) Vol. 243; no. 4891; pp. 629 - 635
• Main Authors: Popham, David L., Szeto, Daniel, Keener, John, Kustu, Sydney
• Format: Journal Article
• Language: English
• Published: Washington, DC The American Association for the Advancement of Science 03-02-1989; American Association for the Advancement of Science
• Subjects: Adenosine Triphosphate - analogs & derivatives; Adenosine Triphosphate - metabolism; Adenosine Triphosphate - pharmacology; Bacteria; Bacterial Proteins; Base Sequence; Binding Sites; Biological and medical sciences; Biology; Deoxyribonuclease I; DNA; DNA binding proteins; DNA, Bacterial - metabolism; DNA-Binding Proteins - metabolism; DNA-Directed RNA Polymerases - metabolism; Enhancer Elements, Genetic; Fundamental and applied biological sciences. Psychology; Gels; Genetic aspects; Genetic transcription; Glutamate-Ammonia Ligase - genetics; Heparin; Heparin - pharmacology; Laws, regulations and rules; Legends; Methylation; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Mutation; Nitrogen metabolism; Nucleotides; Phosphorylation; PII Nitrogen Regulatory Proteins; Promoter regions; Promoter Regions, Genetic; Proteins; RNA; Salmonella typhimurium; Salmonella typhimurium - genetics; Sigma Factor - metabolism; Trans-Activators; Transcription (Genetics); Transcription Factors; Transcription initiation site; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Nitrogen regulatory protein; Transcription; Ternary complex; Enzyme; Binding site; RNA polymerase; Salmonella typhimurium; Enhancer sequence; DNA; Bacteria; Heparin; Methylation; Escherichieae; ATP; Transcription initiation; Enterobacteriaceae
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.2563595

The nitrogen regulatory (NtrC) protein of enteric bacteria, which binds to sites that have the properties of transcriptional enhancers, is known to activate transcription by a form of RNA polymerase that contains the NtrA protein ($\sigma ^{54}$) as sigma factor (referred to as $\sigma ^{54}$-holoenzyme). In the presence of adenosine triphosphate, the NtrC protein catalyzes isomerization of closed recognition complexes between $\sigma ^{54}$-holoenzyme and the glnA promoter to open complexes in which DNA in the region of the transcription start site is locally denatured. NtrC is not required subsequently for maintenance of open complexes or initiation of transcription.