Systematic mutational analysis of the LytTR DNA binding domain of Staphylococcus aureus virulence gene transcription factor AgrA

• Published in: Nucleic acids research Vol. 42; no. 20; pp. 12523 - 12536
• Main Authors: Nicod, Sophie S, Weinzierl, Robert O J, Burchell, Lynn, Escalera-Maurer, Andres, James, Ellen H, Wigneshweraraj, Sivaramesh
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 10.11.2014
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Gene regulation, Chromatin and Epigenetics; Mutagenesis; Mutation; Protein Binding; Protein Structure, Tertiary; Staphylococcus aureus; Staphylococcus aureus - genetics; Staphylococcus aureus - metabolism; Staphylococcus aureus - pathogenicity; Structure-Activity Relationship; Trans-Activators - chemistry; Trans-Activators - genetics; Trans-Activators - metabolism; Transcriptional Activation; Virulence Factors - genetics

Most DNA-binding bacterial transcription factors contact DNA through a recognition α-helix in their DNA-binding domains. An emerging class of DNA-binding transcription factors, predominantly found in pathogenic bacteria interact with the DNA via a relatively novel type of DNA-binding domain, called...