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

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...

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Published inNucleic 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
LanguageEnglish
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
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Abstract 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 to form multimers that condense DNA and restrict gene expression. However, the molecular mechanism through which H-NS senses temperature and other physiochemical parameters remains unclear and controversial. Combining structural, biophysical and computational analyses, we show that human body temperature promotes unfolding of the central dimerization domain, breaking up H-NS multimers. This unfolding event enables an autoinhibitory compact H-NS conformation that blocks DNA binding. Our integrative approach provides the molecular basis for H-NS-mediated environment-sensing and may open new avenues for the control of pathogenic multi-drug resistant bacteria.
AbstractList 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 to form multimers that condense DNA and restrict gene expression. However, the molecular mechanism through which H-NS senses temperature and other physiochemical parameters remains unclear and controversial. Combining structural, biophysical and computational analyses, we show that human body temperature promotes unfolding of the central dimerization domain, breaking up H-NS multimers. This unfolding event enables an autoinhibitory compact H-NS conformation that blocks DNA binding. Our integrative approach provides the molecular basis for H-NS-mediated environment-sensing and may open new avenues for the control of pathogenic multi-drug resistant bacteria.
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 to form multimers that condense DNA and restrict gene expression. However, the molecular mechanism through which H-NS senses temperature and other physiochemical parameters remains unclear and controversial. Combining structural, biophysical and computational analyses, we show that human body temperature promotes unfolding of the central dimerization domain, breaking up H-NS multimers. This unfolding event enables an autoinhibitory compact H-NS conformation that blocks DNA binding. Our integrative approach provides the molecular basis for H-NS-mediated environment-sensing and may open new avenues for the control of pathogenic multi-drug resistant bacteria.
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 to form multimers that condense DNA and restrict gene expression. However, the molecular mechanism through which H-NS senses temperature and other physiochemical parameters remains unclear and controversial. Combining structural, biophysical and computational analyses, we show that human body temperature promotes unfolding of the central dimerization domain, breaking up H-NS multimers. This unfolding event enables an autoinhibitory compact H-NS conformation that blocks DNA binding. Our integrative approach provides the molecular basis for H-NS–mediated environment-sensing and may open new avenues for the control of pathogenic multi-drug resistant bacteria.
Author Li, Yu
Gao, Xin
Cui, Xuefeng
Shahul Hameed, Umar F
Brooks, Claire
Jaremko, Łukasz
Jaremko, Mariusz
Huser, Franceline
Ladbury, John E
Guo, Xianrong
Li, Jianing
Momin, Afaque A
Radhakrishnan, Anand K
Melo, Fernando A
Arold, Stefan T
Aljedani, Safia S
Zhao, Xiaochuan
Liao, Chenyi
AuthorAffiliation 2 Department of Chemistry, The University of Vermont, Burlington, VT 05405, USA
5 King Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering Division (BESE), Thuwal, 23955-6900, Saudi Arabia
4 King Abdullah University of Science and Technology (KAUST), Imaging and Characterization Core Lab, Thuwal, 23955-6900, Saudi Arabia
3 Department of Physics (IBILCE), São Paulo State University, São José do Rio Preto, São Paulo, Brazil
1 King Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Division of Biological and Environmental Sciences and Engineering (BESE), Thuwal, 23955-6900,Saudi Arabia
6 School of Molecular and Cellular Biology, University of Leeds, Leeds, UK
7 King Abdullah University of Science and Technology (KAUST), Division of Biological and Environmental Sciences and Engineering, Thuwal, 23955-6900, Saudi Arabia
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– name: 3 Department of Physics (IBILCE), São Paulo State University, São José do Rio Preto, São Paulo, Brazil
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  surname: Brooks
  fullname: Brooks, Claire
  organization: Department of Chemistry, The University of Vermont, Burlington, VT 05405, USA
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  surname: Li
  fullname: Li, Yu
  email: Jianing.Li@uvm.edu
  organization: King Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering Division (BESE), Thuwal, 23955-6900, Saudi Arabia
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  surname: Arold
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  organization: King Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Division of Biological and Environmental Sciences and Engineering (BESE), Thuwal, 23955-6900,Saudi Arabia
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Snippet Abstract As an environment-dependent pleiotropic gene regulator in Gram-negative bacteria, the H-NS protein is crucial for adaptation and toxicity control of...
As an environment-dependent pleiotropic gene regulator in Gram-negative bacteria, the H-NS protein is crucial for adaptation and toxicity control of human...
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SubjectTerms 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
Title H-NS uses an autoinhibitory conformational switch for environment-controlled gene silencing
URI https://www.ncbi.nlm.nih.gov/pubmed/30597093
https://search.proquest.com/docview/2162496003
https://www.osti.gov/biblio/1489085
https://pubmed.ncbi.nlm.nih.gov/PMC6411929
Volume 47
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