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Protein

DNA-binding protein H-NS

Gene

hns

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A DNA-binding protein implicated in transcriptional repression (silencing) (PubMed:333393, PubMed:2128918, PubMed:8890170, PubMed:8913298, PubMed:9398522, PubMed:16963779, PubMed:17046956, PubMed:23543115). Also involved in bacterial chromosome organization and compaction (PubMed:6379600, PubMed:10982869, PubMed:21903814). H-NS binds tightly to AT-rich dsDNA and inhibits transcription (PubMed:2512122, PubMed:16963779, PubMed:17435766, PubMed:17881364, PubMed:23543115). Binds upstream and downstream of initiating RNA polymerase, trapping it in a loop and preventing transcription (PubMed:11714691). Binds to hundreds of sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome (PubMed:16963779, PubMed:17046956, PubMed:23543115). Many of these loci were horizontally transferred (HTG); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need (PubMed:17046956, PubMed:17881364, PubMed:26789284). Suppresses transcription at many intragenic sites as well as transcription of spurious, non-coding RNAs genome-wide (PubMed:24449106). Repression of HTG by H-NS is thought to allow their DNA to evolve faster than non-H-NS-bound regions, and facilitates integration of HTG into transcriptional regulatory networks (PubMed:26789284). A subset of H-NS/StpA-regulated genes also require Hha (and/or Cnu, ydgT) for repression; Hha and Cnu increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex (PubMed:23543115). The protein forms 2 clusters in the nucleoid which gather hns-bound loci together, bridging non-contiguous DNA, and causes DNA substantial condensation (PubMed:21903814). Binds DNA better at low temperatures than at 37 degrees Celsius; AT-rich sites nucleate H-NS binding, further DNA-binding is cooperative and this cooperativity decreases with rising temperature (PubMed:17435766, PubMed:17881364). Transcriptional repression can be inhibited by dominant-negative mutants of StpA or itself (PubMed:8755860). May effect transcriptional elongation (PubMed:25638302). Can increase translational efficiency of mRNA with suboptimal Shine-Dalgarno sequences (PubMed:20595230). Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD (PubMed:17010156). Plays a role in flagellar function (PubMed:11031114). Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its repression is antagonized by LeuO (PubMed:20132443, PubMed:20659289). Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (PubMed:7934818). Overexpression suppresses secY24, a temperature-sensitive mutation (PubMed:1537791). Has also been reported to activate transcription of some genes (PubMed:4566454, PubMed:338303, PubMed:2128918).1 Publication27 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei12 – 121Interacts with Hha1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi112 – 1176By similarity

GO - Molecular functioni

  • bent DNA binding Source: EcoliWiki
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00288.
ECOL316407:JW1225-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein H-NS1 Publication
Alternative name(s):
Heat-stable nucleoid-structuring protein1 Publication
Histone-like protein HLP-II
Protein B11 Publication
Protein H11 Publication
Gene namesi
Name:hns1 Publication
Synonyms:bglY1 Publication, cur, drdX1 Publication, hnsA, msyA1 Publication, osmZ1 Publication, pilG, topS
Ordered Locus Names:b1237, JW1225
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10457. hns.

Subcellular locationi

  • Cytoplasmnucleoid 2 Publications

  • Note: Forms 2 compact clusters per chromosome, located at one-quarter and three-quarter positions on the cell's long axis: 2 H-NS-repressed genes were closely associated with H-NS clusters while a non-H-NS-repressed gene was not substantially associated with the H-NS cluster (PubMed:21903814).1 Publication

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Decreased growth below 30 degrees Celsius (PubMed:1691451). Altered expression of a number of genes (PubMed:2128918, PubMed:8890170, PubMed:8913298, PubMed:23543115). Derepression of the cryptic blg operon (PubMed:8913298, PubMed:11790731). Alteration of chromosome organization (PubMed:21903814). Double hns-stpA mutants grow slower and have reduced viable cell counts compared to single hns mutants in MC1029 and MC4100 backgrounds (PubMed:8890170). In 0.3M NaCl a double hns-stpA deletion up-regulates 583 and down-regulates 86 genes, 363 of which are thought to have been horizontally acquired; 131 are also up-regulated in a double cnu-hha deletion (PubMed:23543115). At 28 degrees Celsius csgD transcription is reduced (PubMed:17010156). Flagella loss due to reduced expression of the flhDC operon (PubMed:11031114). Flagella can be restored by expression of flhDC, but strains are non-motile, suggesting H-NS also plays a role in flagellar function (PubMed:11031114). Disruption leads to increased expression of CRISPR-cas genes and increased viral resistance (PubMed:20659289).10 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 6968Missing : No longer complements a deletion mutant, has no dominant-negative effects on wild-type protein, does not oligomerize. 1 PublicationAdd
BLAST
Mutagenesisi2 – 2019Missing : No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 1 PublicationAdd
BLAST
Mutagenesisi6 – 61K → P: No effect on oligomerization of N-terminal fragment 1-89. 1 Publication
Mutagenesisi12 – 154RTLR → ERLA: Decreased DNA-binding, loss of preference for curved DNA. 1 Publication
Mutagenesisi12 – 121R → C: Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. 1 Publication
Mutagenesisi12 – 121R → H: Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. Fragments 1-46 and 1-64 no longer bind Hha. 2 Publications
Mutagenesisi12 – 121R → K: Abolishes the interaction with Hha. 1 Publication
Mutagenesisi15 – 151R → C: Derepression of proV and bgl expression. 1 Publication
Mutagenesisi15 – 151R → H: Derepression of proV and bgl expression. Fragments 1-46 and 1-64 fold incorrectly but still bind Hha. 2 Publications
Mutagenesisi17 – 171Q → P: Abolishes oligomerization of N-terminal fragment 1-89. 1 Publication
Mutagenesisi26 – 261L → P: Partial loss of repressor function. 1 Publication
Mutagenesisi30 – 301L → A or K: Wild-type function. 1 Publication
Mutagenesisi30 – 301L → D: Derepression of proV and partial derepression of bgl epxression, does not dimerize, anomalous protein mobility on gels. 1 Publication
Mutagenesisi30 – 301L → P: Derepression of proV and bgl epxression, does not dimerize, anomalous protein mobility on gels. Protein localizes to nucleoid but no longer forms discreet compact clusters. 2 Publications
Mutagenesisi32 – 321K → Q: Loss of Hha binding by fragment 1-64, protein folding is unaffected. 1 Publication
Mutagenesisi53 – 553ERT → GRP: Partial loss of repressor function. 1 Publication
Mutagenesisi54 – 541R → C: Derepression of proV and bgl expression. 1 Publication
Mutagenesisi64 – 13774Missing : No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 2 PublicationsAdd
BLAST
Mutagenesisi90 – 901R → C or H: Derepression of proV expression. 1 Publication
Mutagenesisi91 – 911A → T: Derepression of proV expression. 1 Publication
Mutagenesisi92 – 13746Missing : Derepression of proV expression, loss of DNA-binding, increased oligomerization. No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 2 PublicationsAdd
BLAST
Mutagenesisi93 – 931R → C: Derepression of proV expression. 1 Publication
Mutagenesisi94 – 941P → L or S: Derepression of proV expression. 1 Publication
Mutagenesisi95 – 951A → T: Derepression of proV expression. 1 Publication
Mutagenesisi97 – 971Y → C, H or S: Partial loss of repressor function. 1 Publication
Mutagenesisi110 – 1101T → A: Partial loss of repressor function. 1 Publication
Mutagenesisi110 – 1101T → I: Derepression of proV expression. 1 Publication
Mutagenesisi111 – 1111G → D or S: Derepression of proV expression. 1 Publication
Mutagenesisi113 – 1131G → D: Derepression of proV expression, decreased DNA-binding but still prefers curved DNA, increased oligomerization. 1 Publication
Mutagenesisi113 – 1131G → S: Partial loss of repressor function. 1 Publication
Mutagenesisi114 – 1141R → C or H: Derepression of proV expression. 1 Publication
Mutagenesisi115 – 1151T → I: Derepression of proV expression. 1 Publication
Mutagenesisi116 – 1161P → S: Partial loss of repressor function. Protein localizes to nucleoid but forms about 20-fold fewer localization points. 2 Publications
Mutagenesisi119 – 1191I → T: Partial loss of repressor function. 1 Publication
Mutagenesisi122 – 13716AMDEQ…FLIKQ → KQWMRKVNPSTIS: Partial loss of repressor function. 1 PublicationAdd
BLAST
Mutagenesisi133 – 1331F → S: Partial loss of repressor function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved9 Publications
Chaini2 – 137136DNA-binding protein H-NSPRO_0000168503Add
BLAST

Post-translational modificationi

Cells (strain MRE-600) in mid-exponential phase have three 15.5 kDa proteins with 3 different isoelectric points; the major form (H1a, pI 7.5) rises in concentration during growth while the 2 minor forms (H1b, pI about 7.2 and H1c, pI 7.0) remain approximately constant (PubMed:6379600).1 Publication

Proteomic databases

EPDiP0ACF8.
PaxDbiP0ACF8.
PRIDEiP0ACF8.

2D gel databases

SWISS-2DPAGEP0ACF8.

Expressioni

Inductioni

Protein levels rise from about 4,000/cell in exponential phase to about 18,000/cell in late stationary phase (at protein level) (PubMed:6379600). Subject to transcriptional auto-repression (PubMed:7934818). Induced by increased hydrostatic pressure (PubMed:8226663). hns transcription can be repressed by overexpressed StpA (which is usually repressed by hns) (PubMed:8890170).4 Publications

Gene expression databases

CollecTFiEXPREG_00000830.

Interactioni

Subunit structurei

Homodimer, also found as tetramers or higher oligomers (PubMed:4566454, PubMed:338303, PubMed:3135462, PubMed:8913298, PubMed:9398522, PubMed:8755860, PubMed:12460581, PubMed:23601147). Oligomerizes into higher-order complexes that form bridges between adjacent DNA helices. The N-terminal region (residues 1-64) can interact with overexpressed StpA (PubMed:8755860). Forms a complex with Cnu (YdgT) (PubMed:21600204). The H-NS dimer forms a heterotrimeric complex with Hha in the absence of DNA; this is mediated by residues 1-46 (PubMed:21600204, PubMed:11790731, PubMed:16650431, PubMed:26085102). Interacts with Hfq (PubMed:2020545).1 Publication12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself10EBI-544934,EBI-544934
cnuP644672EBI-544934,EBI-551907
hhaP0ACE35EBI-544934,EBI-1122578
stpAP0ACG13EBI-544934,EBI-551928

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4263496. 32 interactions.
850196. 1 interaction.
DIPiDIP-35853N.
IntActiP0ACF8. 49 interactions.
MINTiMINT-1223907.
STRINGi511145.b1237.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 75Combined sources
Helixi10 – 178Combined sources
Turni18 – 203Combined sources
Helixi24 – 5128Combined sources
Beta strandi97 – 993Combined sources
Beta strandi100 – 1067Combined sources
Turni110 – 1134Combined sources
Beta strandi115 – 1173Combined sources
Helixi118 – 1258Combined sources
Helixi130 – 1323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNRNMR-A91-137[»]
1HNSNMR-A91-137[»]
1LR1NMR-A/B2-58[»]
1NI8NMR-A/B2-47[»]
2MW2NMR-B/C1-46[»]
ProteinModelPortaliP0ACF8.
SMRiP0ACF8. Positions 2-81, 91-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACF8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 6343Involved in dimerization1 PublicationAdd
BLAST
Regioni92 – 13746Required for DNA-binding1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili22 – 49282 PublicationsAdd
BLAST

Domaini

A central region (about residues 21-47) is involved in dimerization, but multimerization requires other residues (PubMed:8755860, PubMed:9398522, PubMed:16650431, PubMed:12460581, PubMed:12592399). The dimerization domain (1-47) also acts as a hinge; changes in its structure probably impact oligomerization and DNA-binding geometries (PubMed:23601147). The N-terminus also interacts with Hha, perhaps via residues 2-18; a well-folded dimer is not necessary for Hha binding (PubMed:16650431). The C-terminus (residues 92-137) binds DNA (PubMed:8913298). Residues in the N-terminus contribute to DNA-binding and to discrimination between curved and non-curved DNA (PubMed:12592399).7 Publications

Sequence similaritiesi

Belongs to the histone-like protein H-NS family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4108SAU. Bacteria.
COG2916. LUCA.
HOGENOMiHOG000218473.
KOiK03746.
OMAiNGVEKTW.
OrthoDBiEOG6NPM97.

Family and domain databases

Gene3Di1.10.287.1050. 1 hit.
4.10.430.10. 1 hit.
InterProiIPR027444. H-NS_C_dom.
IPR001801. Histone_HNS.
IPR027454. Histone_HNS_oligo_dom.
[Graphical view]
PfamiPF00816. Histone_HNS. 1 hit.
[Graphical view]
PIRSFiPIRSF002096. HnS. 1 hit.
SMARTiSM00528. HNS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ACF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE
60 70 80 90 100
VEERTRKLQQ YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV
110 120 130
DENGETKTWT GQGRTPAVIK KAMDEQGKSL DDFLIKQ
Length:137
Mass (Da):15,540
Last modified:January 23, 2007 - v2
Checksum:iE628184AC7C86F49
GO

Mass spectrometryi

Molecular mass is 15407.8 Da from positions 2 - 137. Determined by MALDI. A second experiment gave a mass of 15410.1.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07688 Genomic DNA. Translation: CAA30530.1.
X59940 Genomic DNA. Translation: CAA42565.1.
X57231 Genomic DNA. Translation: CAA40507.1.
X67326 Genomic DNA. Translation: CAA47740.1.
Y00976 Genomic DNA. Translation: CAA68786.1.
U00096 Genomic DNA. Translation: AAC74319.1.
AP009048 Genomic DNA. Translation: BAA36117.1.
PIRiS00903.
RefSeqiNP_415753.1. NC_000913.3.
WP_001287378.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74319; AAC74319; b1237.
BAA36117; BAA36117; BAA36117.
GeneIDi945829.
KEGGiecj:JW1225.
eco:b1237.
PATRICi32117730. VBIEscCol129921_1285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07688 Genomic DNA. Translation: CAA30530.1.
X59940 Genomic DNA. Translation: CAA42565.1.
X57231 Genomic DNA. Translation: CAA40507.1.
X67326 Genomic DNA. Translation: CAA47740.1.
Y00976 Genomic DNA. Translation: CAA68786.1.
U00096 Genomic DNA. Translation: AAC74319.1.
AP009048 Genomic DNA. Translation: BAA36117.1.
PIRiS00903.
RefSeqiNP_415753.1. NC_000913.3.
WP_001287378.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNRNMR-A91-137[»]
1HNSNMR-A91-137[»]
1LR1NMR-A/B2-58[»]
1NI8NMR-A/B2-47[»]
2MW2NMR-B/C1-46[»]
ProteinModelPortaliP0ACF8.
SMRiP0ACF8. Positions 2-81, 91-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263496. 32 interactions.
850196. 1 interaction.
DIPiDIP-35853N.
IntActiP0ACF8. 49 interactions.
MINTiMINT-1223907.
STRINGi511145.b1237.

2D gel databases

SWISS-2DPAGEP0ACF8.

Proteomic databases

EPDiP0ACF8.
PaxDbiP0ACF8.
PRIDEiP0ACF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74319; AAC74319; b1237.
BAA36117; BAA36117; BAA36117.
GeneIDi945829.
KEGGiecj:JW1225.
eco:b1237.
PATRICi32117730. VBIEscCol129921_1285.

Organism-specific databases

EchoBASEiEB0452.
EcoGeneiEG10457. hns.

Phylogenomic databases

eggNOGiENOG4108SAU. Bacteria.
COG2916. LUCA.
HOGENOMiHOG000218473.
KOiK03746.
OMAiNGVEKTW.
OrthoDBiEOG6NPM97.

Enzyme and pathway databases

BioCyciEcoCyc:PD00288.
ECOL316407:JW1225-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ACF8.
PROiP0ACF8.

Gene expression databases

CollecTFiEXPREG_00000830.

Family and domain databases

Gene3Di1.10.287.1050. 1 hit.
4.10.430.10. 1 hit.
InterProiIPR027444. H-NS_C_dom.
IPR001801. Histone_HNS.
IPR027454. Histone_HNS_oligo_dom.
[Graphical view]
PfamiPF00816. Histone_HNS. 1 hit.
[Graphical view]
PIRSFiPIRSF002096. HnS. 1 hit.
SMARTiSM00528. HNS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, cloning, nucleotide sequence and chromosomal map location of hns, the structural gene for Escherichia coli DNA-binding protein H-NS."
    Pon C.L., Calogero R.A., Gualerzi C.O.
    Mol. Gen. Genet. 212:199-202(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS."
    Falconi M., Gualtieri M.T., la Teana A., Losso M.A., Pon C.L.
    Mol. Microbiol. 2:323-329(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
  3. "Transcriptional silencing and thermoregulation of gene expression in Escherichia coli."
    Goeransson M., Sonden B., Nilsson P., Dagberg B., Forsman K., Emanuelsson K., Uhlin B.E.
    Nature 344:682-685(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
  4. "Multicopy suppression: an approach to understanding intracellular functioning of the protein export system."
    Ueguchi C., Ito K.
    J. Bacteriol. 174:1454-1461(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: K12.
  5. "The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a component of the Escherichia coli K12 nucleoid."
    May G., Dersch P., Haardt M., Middendorf A., Bremer E.
    Mol. Gen. Genet. 224:81-90(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC4100.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Filling the gap between hns and adhE in Escherichia coli K12."
    Danchin A., Krin E.
    Microbiology 141:959-960(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
    Strain: K12.
  10. "Characterization of the structural genes for the DNA-binding protein H-NS in Enterobacteriaceae."
    la Teana A., Falconi M., Scarlato V., Lammi M., Pon C.L.
    FEBS Lett. 244:34-38(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
  11. "Identification and sequence determination of the host factor gene for bacteriophage Q beta."
    Kajitani M., Ishihama A.
    Nucleic Acids Res. 19:1063-1066(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-27, SUBUNIT.
    Strain: P4X8 / ME7784.
  12. "A DNA-binding protein from E. coli isolation, characterization and its relationship with proteins H1 and B1."
    Laine B., Sautiere P., Spassky A., Rimsky S.
    Biochem. Biophys. Res. Commun. 119:1147-1153(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, DNA-BINDING.
    Strain: MRE-600.
  13. "An Escherichia coli protein that preferentially binds to sharply curved DNA."
    Yamada H., Muramatsu S., Mizuno T.
    J. Biochem. 108:420-425(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20, DNA-BINDING.
  14. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
    Strain: K12.
  15. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  16. Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  17. "Proteins from the prokaryotic nucleoid: biochemical and 1H NMR studies on three bacterial histone-like proteins."
    Lammi M., Paci M., Pon C.L., Losso M.A., Miano A., Pawlik R.T., Gianfranceschi G.L., Gualerzi C.O.
    Adv. Exp. Med. Biol. 179:467-477(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8, DNA-BINDING, PROTEIN NAME.
  18. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  19. "Two heat-resistant, low molecular weight proteins from Escherichia coli that stimulate DNA-directed RNA synthesis."
    Cukier-Kahn R., Jacquet M., Gros F.
    Proc. Natl. Acad. Sci. U.S.A. 69:3643-3647(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DNA-BINDING.
    Strain: MRE-600.
  20. "Histone-like proteins in the purified Escherichia coli deoxyribonucleoprotein."
    Varshavsky A.J., Nedospasov S.A., Bakayev V.V., Bakayeva T.G., Georgiev G.P.
    Nucleic Acids Res. 4:2725-2745(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING.
    Strain: 802.
  21. "Physico-chemical properties of a DNA binding protein: Escherichia coli factor H1."
    Spassky A., Buc H.C.
    Eur. J. Biochem. 81:79-90(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DNA-BINDING.
    Strain: MRE-600.
  22. "H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro."
    Spassky A., Rimsky S., Garreau H., Buc H.
    Nucleic Acids Res. 12:5321-5340(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, POST-TRANSLATIONAL MODIFICATION, DNA-BINDING.
    Strain: MRE-600.
  23. "Synthetic curved DNA sequences can act as transcriptional activators in Escherichia coli."
    Bracco L., Kotlarz D., Kolb A., Diekmann S., Buc H.
    EMBO J. 8:4289-4296(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING OF CURVED DNA.
  24. "Mutations in bglY, the structural gene for the DNA-binding protein H1, affect expression of several Escherichia coli genes."
    Bertin P., Lejeune P., Laurent-Winter C., Danchin A.
    Biochimie 72:889-891(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12.
  25. "Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression."
    Falconi M., Higgins P.N., Spurio R., Pon C.L., Gualerzi C.O.
    Mol. Microbiol. 10:273-282(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DNA-BINDING.
  26. "Stress response of Escherichia coli to elevated hydrostatic pressure."
    Welch T.J., Farewell A., Neidhardt F.C., Bartlett D.H.
    J. Bacteriol. 175:7170-7177(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  27. "Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using dominant negative derivatives."
    Williams R.M., Rimsky S., Buc H.
    J. Bacteriol. 178:4335-4343(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-26; 53-GLU--THR-55; 64-MET--GLN-137; TYR-97; THR-110; GLY-113; PRO-116; ILE-119; 122-ALA--GLN-137 AND PHE-133.
  28. "Coordinated and differential expression of histone-like proteins in Escherichia coli: regulation and function of the H-NS analog StpA."
    Sonden B., Uhlin B.E.
    EMBO J. 15:4970-4980(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: K12, K12 / MC1029 and K12 / MC4100 / ATCC 35695 / DSM 6574.
  29. "Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS."
    Ueguchi C., Suzuki T., Yoshida T., Tanaka K., Mizuno T.
    J. Mol. Biol. 263:149-162(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-12; ARG-15; ARG-54; ARG-90; ALA-91; 92-GLN--GLN-137; ARG-93; PRO-94; ALA-95; THR-110; GLY-111; ARG-114 AND THR-115.
    Strain: K12 / CSH26.
  30. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  31. "Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS."
    Ueguchi C., Seto C., Suzuki T., Mizuno T.
    J. Mol. Biol. 274:145-151(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF 2-SER--GLY-69; 2-SER--GLU-20; LEU-30; 64-MET--GLN-137 AND 92-GLN--GLN-137.
  32. "H-NS mediated compaction of DNA visualised by atomic force microscopy."
    Dame R.T., Wyman C., Goosen N.
    Nucleic Acids Res. 28:3504-3510(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA COMPACTION, DNA-BINDING.
  33. "Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli."
    Ko M., Park C.
    J. Mol. Biol. 303:371-382(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FLAGELLA BIOGENESIS AND MOTILITY, DISRUPTION PHENOTYPE.
    Strain: K12.
  34. "Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1."
    Dame R.T., Wyman C., Wurm R., Wagner R., Goosen N.
    J. Biol. Chem. 277:2146-2150(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE MECHANISM OF TRANSCRIPTIONAL REPRESSION.
  35. "Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins."
    Nieto J.M., Madrid C., Miquelay E., Parra J.L., Rodriguez S., Juarez A.
    J. Bacteriol. 184:629-635(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHA, MASS SPECTROMETRY, DISRUPTION PHENOTYPE.
  36. "New roles for key residues in helices H1 and H2 of the Escherichia coli H-NS N-terminal domain: H-NS dimer stabilization and Hha binding."
    Garcia J., Madrid C., Juarez A., Pons M.
    J. Mol. Biol. 359:679-689(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-12 AND ARG-15.
  37. "Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome."
    Grainger D.C., Hurd D., Goldberg M.D., Busby S.J.
    Nucleic Acids Res. 34:4642-4652(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REGULON, DNA-BINDING.
    Strain: K12 / MG1655 / ATCC 47076.
  38. "Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase."
    Oshima T., Ishikawa S., Kurokawa K., Aiba H., Ogasawara N.
    DNA Res. 13:141-153(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SILENCING OF FOREIGN DNA, REGULON, DNA-BINDING.
    Strain: K12 / MG1655 / ATCC 47076.
  39. "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli."
    Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.
    Mol. Microbiol. 62:1014-1034(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN CURLI FIMBRIAE EXPRESSION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100.
  40. "H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing."
    Bouffartigues E., Buckle M., Badaut C., Travers A., Rimsky S.
    Nat. Struct. Mol. Biol. 14:441-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  41. "High-affinity DNA binding sites for H-NS provide a molecular basis for selective silencing within proteobacterial genomes."
    Lang B., Blot N., Bouffartigues E., Buckle M., Geertz M., Gualerzi C.O., Mavathur R., Muskhelishvili G., Pon C.L., Rimsky S., Stella S., Babu M.M., Travers A.
    Nucleic Acids Res. 35:6330-6337(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MODEL OF ACTION, DNA-BINDING.
  42. "Identification and characterization of E. coli CRISPR-cas promoters and their silencing by H-NS."
    Pul U., Wurm R., Arslan Z., Geissen R., Hofmann N., Wagner R.
    Mol. Microbiol. 75:1495-1512(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REPRESSING CRISPR EXPRESSION.
    Strain: K12.
  43. "Novel role for a bacterial nucleoid protein in translation of mRNAs with suboptimal ribosome-binding sites."
    Park H.S., Ostberg Y., Johansson J., Wagner E.G., Uhlin B.E.
    Genes Dev. 24:1345-1350(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSLATION ACTIVATION, MRNA-BINDING.
  44. "H-NS-mediated repression of CRISPR-based immunity in Escherichia coli K12 can be relieved by the transcription activator LeuO."
    Westra E.R., Pul U., Heidrich N., Jore M.M., Lundgren M., Stratmann T., Wurm R., Raine A., Mescher M., Van Heereveld L., Mastop M., Wagner E.G., Schnetz K., Van Der Oost J., Wagner R., Brouns S.J.
    Mol. Microbiol. 77:1380-1393(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ANTAGONIZED BY LEUO, ROLE IN CRISPR EXPRESSION, DISRUPTION PHENOTYPE.
    Strain: K12.
  45. "Essential residues in the H-NS binding site of Hha, a co-regulator of horizontally acquired genes in Enterobacteria."
    de Alba C.F., Solorzano C., Paytubi S., Madrid C., Juarez A., Garcia J., Pons M.
    FEBS Lett. 585:1765-1770(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHA AND CNU (YDGT), MUTAGENESIS OF ARG-12.
    Strain: K12 / MG1655 / ATCC 47076.
  46. "Chromosome organization by a nucleoid-associated protein in live bacteria."
    Wang W., Li G.W., Chen C., Xie X.S., Zhuang X.
    Science 333:1445-1449(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CHROMOSOME ORGANIZATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LEU-30 AND PRO-116.
    Strain: K12 / BW25993.
  47. "Functions of the Hha and YdgT proteins in transcriptional silencing by the nucleoid proteins, H-NS and StpA, in Escherichia coli."
    Ueda T., Takahashi H., Uyar E., Ishikawa S., Ogasawara N., Oshima T.
    DNA Res. 20:263-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REGULON, DISRUPTION PHENOTYPE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  48. "Widespread suppression of intragenic transcription initiation by H-NS."
    Singh S.S., Singh N., Bonocora R.P., Fitzgerald D.M., Wade J.T., Grainger D.C.
    Genes Dev. 28:214-219(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
    Strain: K12 / MG1655 / ATCC 47076.
  49. "H-NS facilitates sequence diversification of horizontally transferred DNAs during their integration in host chromosomes."
    Higashi K., Tobe T., Kanai A., Uyar E., Ishikawa S., Suzuki Y., Ogasawara N., Kurokawa K., Oshima T.
    PLoS Genet. 12:E1005796-E1005796(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  50. "Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli."
    Shindo H., Iwaki T., Ieda R., Kurumizaka H., Ueguchi C., Mizuno T., Morikawa S., Nakamura H., Kuboniwa H.
    FEBS Lett. 360:125-131(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 91-137.
  51. "H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein."
    Esposito D., Petrovic A., Harris R., Ono S., Eccleston J.F., Mbabaali A., Haq I., Higgins C.F., Hinton J.C., Driscoll P.C., Ladbury J.E.
    J. Mol. Biol. 324:841-850(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-58, DOMAIN, MUTAGENESIS OF LYS-6 AND GLN-17, COILED COIL.
  52. "The H-NS dimerization domain defines a new fold contributing to DNA recognition."
    Bloch V., Yang Y., Margeat E., Chavanieu A., Auge M.T., Robert B., Arold S., Rimsky S., Kochoyan M.
    Nat. Struct. Biol. 10:212-218(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-47, DOMAIN, MUTAGENESIS OF 12-ARG--ARG-15, COILED COIL.
  53. "Protein oligomers studied by solid-state NMR--the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein."
    Renault M., Garcia J., Cordeiro T.N., Baldus M., Pons M.
    FEBS J. 280:2916-2928(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY SOLID STATE NMR, SUBUNIT, DOMAIN.
  54. "A three-protein charge zipper stabilizes a complex modulating bacterial gene silencing."
    Cordeiro T.N., Garcia J., Bernado P., Millet O., Pons M.
    J. Biol. Chem. 290:21200-21212(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-46 IN COMPLEX WITH HHA, SUBUNIT, MUTAGENESIS OF LYS-32.
  55. "H-NS and RNA polymerase: a love-hate relationship?"
    Landick R., Wade J.T., Grainger D.C.
    Curr. Opin. Microbiol. 24:53-59(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiHNS_ECOLI
AccessioniPrimary (citable) accession number: P0ACF8
Secondary accession number(s): P08936, Q47267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.