Histone-like nucleoid-structuring protein

In molecular biology, the histone-like nucleoid-structuring (H-NS) protein belongs to a family of bacterial proteins that play a role in the formation of nucleoid structure and affect gene expression under certain conditions.[1] The protein has a homologue that is encoded by many large, conjugative plasmids.[2]

H-NS histone family
solution structure of the oligomerization domain of the bacterial chromatin-structuring protein h-ns
Identifiers
SymbolHistone_HNS
PfamPF00816
InterProIPR001801
SCOPe1hns / SUPFAM

Mechanism

A major function of H-NS is to influence DNA topology. It is believed that H-NS achieves this by forming complexes with itself and binding to different sections of DNA, bringing them together.[3][4] Another major role of H-NS is to turn off the expression of genes. H-NS regulates gene expression by binding to AT rich DNA, which is a common feature of promoters, and of horizontally acquired genes.[5] Relief of suppression by H-NS can be achieved by the binding of another protein, or by changes in DNA topology which can occur due to changes in temperature and osmolarity, for example.[3]

H-NS can also interact with other proteins and influence their function, for example it can interact with the flagellar motor protein FliG to increase its activity.[6]

gollark: Which I disagree with, yes.
gollark: If it became possible to grow babies externally or conveniently move them, that might be an acceptable solution too.
gollark: To rethingy: I think that, regardless of whose body or creation or whatever it is, the person who is actually carrying it and bears the associated issues of having it glued to their circulatory system and such should get to decide whether to keep doing that.
gollark: A fetus contains some of your genes but ~all of its materials come from what the mother eats/processes, so that isn't relevant either.
gollark: I'll rephrase a bit or something.

References
  1. Shindo H, Iwaki T, Ieda R, Kurumizaka H, Ueguchi C, Mizuno T, Morikawa S, Nakamura H, Kuboniwa H (February 1995). "Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli". FEBS Lett. 360 (2): 125–31. doi:10.1016/0014-5793(95)00079-O. PMID 7875316.
  2. Beloin, C.; Deighan, P.; Doyle, M.; Dorman, C. J. (2003-10-01). "Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein". Molecular genetics and genomics: MGG. 270 (1): 66–77. doi:10.1007/s00438-003-0897-0. ISSN 1617-4615. PMID 12898223.
  3. Dorman, Charles J. (May 2004). "H-NS: a universal regulator for a dynamic genome". Nature Reviews Microbiology. 2 (5): 391–400. doi:10.1038/nrmicro883.
  4. Dame, RT; Wyman, C; Goosen, N (15 September 2000). "H-NS mediated compaction of DNA visualised by atomic force microscopy". Nucleic Acids Research. 28 (18): 3504–10. doi:10.1093/nar/28.18.3504. PMC 110753. PMID 10982869.
  5. Lucchini, Sacha; Rowley, Gary; Goldberg, Martin D.; Hurd, Douglas; Harrison, Marcus; Hinton, Jay C. D. (2006). "H-NS Mediates the Silencing of Laterally Acquired Genes in Bacteria". PLoS Pathogens. 2 (8): e81. doi:10.1371/journal.ppat.0020081. PMC 1550270. PMID 16933988.
  6. Donato, Gina M.; Kawula, Thomas H. (11 September 1998). "Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in". Journal of Biological Chemistry. 273 (37): 24030–24036. doi:10.1074/jbc.273.37.24030.
This article incorporates text from the public domain Pfam and InterPro: IPR001801


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