H-NS uses an autoinhibitory conformational switch for environment-controlled gene silencing

• Published in: Nucleic acids research Vol. 47; no. 5; pp. 2666 - 2680
• Main Authors: Shahul Hameed, Umar F, Liao, Chenyi, Radhakrishnan, Anand K, Huser, Franceline, Aljedani, Safia S, Zhao, Xiaochuan, Momin, Afaque A, Melo, Fernando A, Guo, Xianrong, Brooks, Claire, Li, Yu, Cui, Xuefeng, Gao, Xin, Ladbury, John E, Jaremko, Łukasz, Jaremko, Mariusz, Li, Jianing, Arold, Stefan T
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 18.03.2019
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - genetics; DNA, Bacterial - chemistry; DNA, Bacterial - genetics; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; Enterohemorrhagic Escherichia coli - genetics; Enterohemorrhagic Escherichia coli - pathogenicity; Gene-Environment Interaction; Humans; Protein Domains; Protein Multimerization - genetics; Protein Unfolding; Salmonella - genetics; Salmonella - pathogenicity; Structural Biology; Temperature; Vibrio cholerae - genetics; Vibrio cholerae - pathogenicity

Abstract As an environment-dependent pleiotropic gene regulator in Gram-negative bacteria, the H-NS protein is crucial for adaptation and toxicity control of human pathogens such as Salmonella, Vibrio cholerae or enterohaemorrhagic Escherichia coli. Changes in temperature affect the capacity of H-NS...