Mechanisms of Toxin Inhibition and Transcriptional Repression by Escherichia coli DinJ-YafQ

• Published in: The Journal of biological chemistry Vol. 289; no. 30; pp. 20559 - 20569
• Main Authors: Ruangprasert, Ajchareeya, Maehigashi, Tatsuya, Miles, Stacey J., Giridharan, Nisha, Liu, Julie X., Dunham, Christine M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25.07.2014; American Society for Biochemistry and Molecular Biology
• Subjects: Bacterial Toxin; Bacterial Toxins - chemistry; Bacterial Toxins - genetics; Bacterial Toxins - metabolism; Crystallography, X-Ray; Energy Metabolism; Escherichia coli - chemistry; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Gene Regulation; Models, Biological; Protein Multimerization - physiology; Protein Structure, Quaternary; Repressor Proteins - chemistry; Repressor Proteins - genetics; Repressor Proteins - metabolism; Ribbon-Helix-Helix Factor; Stress Response; Toxin-Antitoxin Complexes; Transcription Repressor; Transcription, Genetic - physiology; X-ray Crystallography; Energy Metabolism; X-ray Crystallography; Stress Response; Transcription Repressor; Toxin-Antitoxin Complexes; Bacterial Toxin; Ribbon-Helix-Helix Factor

Bacteria encounter environmental stresses that regulate a gene expression program required for adaptation and survival. Here, we report the 1.8-Å crystal structure of the Escherichia coli toxin-antitoxin complex YafQ-(DinJ)2-YafQ, a key component of the stress response. The antitoxin DinJ dimer adop...