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19  structures 1332  species 1  interaction 2751  sequences 9  architectures

Family: Histone_HNS (PF00816)

Summary: H-NS histone family

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This is the Wikipedia entry entitled "Histone-like nucleoid-structuring protein". More...

Histone-like nucleoid-structuring protein Edit Wikipedia article

H-NS histone family
PDB 1lr1 EBI.jpg
solution structure of the oligomerization domain of the bacterial chromatin-structuring protein h-ns
Identifiers
Symbol Histone_HNS
Pfam PF00816
InterPro IPR001801
SCOP 1hns
SUPERFAMILY 1hns

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]

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]

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. ^ a b 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. 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. 
  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


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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Literature references

  1. Shindo H, Iwaki T, Ieda R, Kurumizaka H, Ueguchi C, Mizuno T, Morikawa S, Nakamura H, Kuboniwa H;, , FEBS Lett 1995;360:125-131.: Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. PUBMED:7875316 EPMC:7875316


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001801

The histone-like nucleoid-structuring (H-NS) protein is a DNA-binding protein implicated in transcriptional repression (silencing) as well as in bacterial chromosome organisation [PUBMED:7875316]. H-NS binds tightly to AT-rich dsDNA, increases its thermal stability and inhibits transcription. It also binds to ssDNA and RNA but with a much lower affinity [PUBMED:18387844].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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(214)
Full
(2751)
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(10226)
NCBI
(13293)
Meta
(133)
RP15
(282)
RP35
(1366)
RP55
(2714)
RP75
(4979)
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  Seed
(214)
Full
(2751)
Representative proteomes UniProt
(10226)
NCBI
(13293)
Meta
(133)
RP15
(282)
RP35
(1366)
RP55
(2714)
RP75
(4979)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(214)
Full
(2751)
Representative proteomes UniProt
(10226)
NCBI
(13293)
Meta
(133)
RP15
(282)
RP35
(1366)
RP55
(2714)
RP75
(4979)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1651 (release 2.1)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 214
Number in full: 2751
Average length of the domain: 90.40 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 76.78 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.9 23.9
Trusted cut-off 23.9 23.9
Noise cut-off 23.8 23.8
Model length: 92
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

Histone_HNS

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Histone_HNS domain has been found. There are 19 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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