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Bdira FB, Erkelens AM, Qin L, et al. Novel anti-repression mechanism of H-NS proteins by a phage protein. Nucleic Acids Res. 2021;49(18):10770-10784doi: 10.1093/nar/gkab793.
Bdira, F. B., Erkelens, A. M., Qin, L., Volkov, A. N., Lippa, A. M., Bowring, N., Boyle, A. L., Ubbink, M., Dove, S. L., & Dame, R. T. (2021). Novel anti-repression mechanism of H-NS proteins by a phage protein. Nucleic acids research, 49(18), 10770-10784. https://doi.org/10.1093/nar/gkab793
Bdira, Fredj Ben, et al. "Novel anti-repression mechanism of H-NS proteins by a phage protein." Nucleic acids research vol. 49,18 (2021): 10770-10784. doi: https://doi.org/10.1093/nar/gkab793
Bdira FB, Erkelens AM, Qin L, Volkov AN, Lippa AM, Bowring N, Boyle AL, Ubbink M, Dove SL, Dame RT. Novel anti-repression mechanism of H-NS proteins by a phage protein. Nucleic Acids Res. 2021 Oct 11;49(18):10770-10784. doi: 10.1093/nar/gkab793. PMID: 34520554; PMCID: PMC8501957.
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Nucleic Acids Res. 2021 Oct 11;49(18):10770-10784. doi: 10.1093/nar/gkab793.

Novel anti-repression mechanism of H-NS proteins by a phage protein.

Nucleic acids research

Fredj Ben Bdira, Amanda M Erkelens, Liang Qin, Alexander N Volkov, Andrew M Lippa, Nicholas Bowring, Aimee L Boyle, Marcellus Ubbink, Simon L Dove, Remus T Dame

Affiliations

  1. Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
  2. Centre for Microbial Cell Biology, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
  3. VIB-VUB Structural Biology Research Center, Pleinlaan 2, 1050 Brussels, Belgium.
  4. Jean Jeener NMR Centre, VUB, Pleinlaan 2, 1050 Brussels, Belgium.
  5. Boston Children's Hospital, Division of Infectious Diseases, Harvard Medical School, Boston, MA 02115, USA.

PMID: 34520554 PMCID: PMC8501957 DOI: 10.1093/nar/gkab793

Abstract

H-NS family proteins, bacterial xenogeneic silencers, play central roles in genome organization and in the regulation of foreign genes. It is thought that gene repression is directly dependent on the DNA binding modes of H-NS family proteins. These proteins form lateral protofilaments along DNA. Under specific environmental conditions they switch to bridging two DNA duplexes. This switching is a direct effect of environmental conditions on electrostatic interactions between the oppositely charged DNA binding and N-terminal domains of H-NS proteins. The Pseudomonas lytic phage LUZ24 encodes the protein gp4, which modulates the DNA binding and function of the H-NS family protein MvaT of Pseudomonas aeruginosa. However, the mechanism by which gp4 affects MvaT activity remains elusive. In this study, we show that gp4 specifically interferes with the formation and stability of the bridged MvaT-DNA complex. Structural investigations suggest that gp4 acts as an 'electrostatic zipper' between the oppositely charged domains of MvaT protomers, and stabilizes a structure resembling their 'half-open' conformation, resulting in relief of gene silencing and adverse effects on P. aeruginosa growth. The ability to control H-NS conformation and thereby its impact on global gene regulation and growth might open new avenues to fight Pseudomonas multidrug resistance.

© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

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