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Escherichia coli K-12 substr. MG1655 Polypeptide: H-NS DNA-binding transcriptional dual regulator



Gene: hns Accession Numbers: EG10457 (EcoCyc), b1237, ECK1232

Synonyms: B1, H1, virR, topX, topS, pilG, osmZ, msyA, irk, hnsA, bglY, cur, drc, drdX, drs, fimG, DNA-binding protein HLP-II (HU, BH2, HD, NS), H-NS

Regulation Summary Diagram: ?

Summary:
The H-NS protein, for "Histone-like nucleoid structuring protein," is a nucleoid-associated multifunctional protein that is capable of condensing [Dame00] and supercoiling DNA [Zimmerman06, Dame05, McLeod01, Tupper94]. It is a global transcriptional silencer of genes with high AT content [Dorman04, Fang08], regulates 5% of all Escherichia coli genes [Hommais01], and plays a key role in global chromosome organization in bacteria [Wang11c]. This protein acts as a pleiotropic transcriptional factor with a strong preference for horizontally acquired genes among the 250 loci to which it binds [Yamada90, Oshima06]. H-NS functions almost exclusively as a transcriptional repressor, although there is no clear evidence that this regulator is an activator. Currently, no inducer for this regulator has been reported in the literature, although Reush et al. proposed that this regulator can form a complex with a short chain of polyhydroxybutyrate [Reusch02]. Additional genes might be identified by high-throughput analysis [Uyar09].

H-NS plays an important role in the regulation of many genes in response to environmental changes and adaptation to stress; therefore, it is capable of controlling its own synthesis [Falconi93, Falconi96]. It also regulates transcription of many other genes that participate in a variety of cellular functions, including genes involved in the following processes or responses: biogenesis of flagella [Bertin94, Soutourina99, Landini02], transcription control of the type I fimbria structural genes [Donato99, Donato97, Olsen98, Olsen94, Schembri98], acid resistance [Shin05], the functional glutamic acid-dependent system [De99], osmotically inducible genes [Bouvier98], the glutamate decarboxylase-dependent acid resistance system [Giangrossi05, Ma02, Tramonti02, Hommais01], osmotic control [Lucht94, Rajkumari01], the type II secretion pathway [Francetic00a], carbon sources [Rimsky90], genes involved in the RNA component of the small subunit (30S subunit) [Afflerbach98, Gralla05], and proteases [Forns05], among others. It has also been shown to be involved in survival during stationary phase, conferring to the bacteria a growth advantage during stationary phase (GASP) [Chib12].

H-NS is capable of inducing severe bends in the DNA, interacting with a large number of DNA regions that contain a planar curvature [Yamada90, Yamada91, Jauregui03]. It has been suggested that H-NS binds strongly to sites carrying a 10-bp AT-rich consensus sequence, which functions as a nucleation site for the formation of a repressive higher-order nucleoprotein complex [Lang07, Sette09]. H-NS binds to intergenic regions as well as regions within genes, but not all genes that bind H-NS are affected by this protein, a fact that is in agreement with the primary role assigned to HN-S in maintenance of nucleoid structure. Currently, there are different models for the formation of DNA-H-NS-DNA bridges which show that this protein binds in tandem to sequences in the genome, forming multimers [Dame05, Dorman07, Luijsterburg06].

As expected for a gene involved in the modulation of many cellular processes, the expression of hns is regulated by several systems and at different levels. At the transcription level, hns is autoregulated, and it is controlled by different transcription factors. hns is induced by high hydrostatic pressure [Welch93a] and DNA synthesis [Free95]. At the posttranscriptional level, it is subject to regulation by the sRNAs Hfq and DsrA [Lease00, Brescia03, Majdalani05, Brescia04, Repoila03a].

It is a DNA-binding protein with similarity to StpA [Shi94, Zhang92] and these two proteins can have similar functions [Ali99, Azam00]. It has an approximately fivefold-lower affinity for DNA than StpA and has a major preference for curved DNA [Sonnenfield01]. StpA appears to be a backup for Hns in the regulation of a set of nonessential and recently acquired genes [Srinivasan13].

Expression of stpA from a plasmid can complement an hns mutant phenotype and StpA is able to repress and activate a subset of H-NS-regulated genes, but the specific mechanisms remain to be determined [Shi94, Sonnenfield01, Sonden96, Zhang96, Uyar09, Sonden96]. A dominant negative form of StpA can disrupt H-NS activity and vice versa, and H-NS can interact with StpA at two distinct domains to form heterodimers in vitro; also, there is evidence that these proteins can form homodimers [Johansson01, Williams96a, Dorman99, Williams96a]. For this reason, in the absence of H-NS the StpA protein is rapidly degraded in a Lon protease-dependent manner [Johansson01, Johansson99]; protection from proteolytic degradation appears to be mediated by a direct interaction between StpA and H-NS [Johansson01]. On the other hand H-NS also may form heterotrimeric complexes with Hha and YdgT [Madrid07, Paytubi04]. It was proposed that Hha enhances the oligomerization of Hns/StpA which is necessary to form DNA-protein filaments to repress transcription [Ueda13, Renault13]. The high-resolution structure based on solid-state NMR spectra from full-length H-NS has been determined [Renault13].

H-NS is a small protein and it is an abundant nucleic acid protein in the genome, with about 20,000 copies per cell. This regulator belongs to the histone-like family of transcriptional regulators and the structure of the protein consists of two structured domains which are separated by a flexible linker [Dorman04]. The N-terminal domain is required for oligomerization and it is involved in protein-protein interactions, while the purified C-terminal domain is involved in DNA binding [Dorman04, Dorman99, Williams96a, Rimsky04, Sette09]. The cooperative binding of H-NS to DNA is related to protein-protein interactions [Giangrossi14].

H-NS forms two compact clusters associated with each copy of the chromosome. These clusters are located near the one-quarter and three-quarter positions along the long axis of the cell [Wang11c]. In cells with three clusters, the additional cluster tends to appear in the middle [Wang11c]. The two cluster formations are induced by the N-terminal domain-driven oligomerization of the protein [Wang11c]. H-NS sequesters the regulated genes and operons into these clusters and juxtaposed numerous DNA segments broadly distributed throughout the chromosome [Wang11c]. Wang et al. (2011) reported that H-NS clusters could thus serve as anchoring points for numerous DNA loci distributed throughout the genome, creating DNA loops connecting the anchored loci [Wang11c].

It was found that the promoter islands, which are regions of DNA containing multiple transcription start sites, are recognized and inactivated by HNS. These promoter islands are associated with genes acquired horizontally [Panyukov13].

Based on ChIP-chip and chip-seq analysis, it was proved that Rho-dependent termination abrogates the H-NS-DNA interactions, leading to transcriptional derepression of H-NS-silenced genes [Chandraprakash14].

Reviews: [Luijsterburg06, Dorman07, Dame05, Williams97, Dorman04, Repoila03a].

Citations: [Laine84, Falconi88, Pon88, Goransson90, May90, Kajitani91, Ueguchi92, Ueguchi93, Ussery94]

Gene Citations: [Ueguchi93]

Locations: cytosol, membrane

Map Position: [1,291,732 <- 1,292,145] (27.84 centisomes)
Length: 414 bp / 137 aa

Molecular Weight of Polypeptide: 15.54 kD (from nucleotide sequence)

pI: 5.37

Unification Links: ASAP:ABE-0004152 , CGSC:960 , DIP:DIP-35853N , EchoBASE:EB0452 , EcoGene:EG10457 , EcoliWiki:b1237 , Mint:MINT-1223907 , OU-Microarray:b1237 , PortEco:hns , PR:PRO_000022909 , Pride:P0ACF8 , Protein Model Portal:P0ACF8 , RefSeq:NP_415753 , RegulonDB:EG10457 , SMR:P0ACF8 , String:511145.b1237 , UniProt:P0ACF8

Relationship Links: InterPro:IN-FAMILY:IPR001801 , InterPro:IN-FAMILY:IPR027444 , InterPro:IN-FAMILY:IPR027454 , PDB:Structure:1HNR , PDB:Structure:1HNS , PDB:Structure:1LR1 , PDB:Structure:1NI8 , Pfam:IN-FAMILY:PF00816 , Smart:IN-FAMILY:SM00528

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006351 - transcription, DNA-templated Inferred by computational analysis [UniProtGOA11]
GO:0006355 - regulation of transcription, DNA-templated Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0003681 - bent DNA binding Inferred from experiment [Azam99]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06, deAlba11, Butland05]
GO:0042802 - identical protein binding Inferred from experiment [Ueguchi97, Stella06, Bloch03]
GO:0003677 - DNA binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0046983 - protein dimerization activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005737 - cytoplasm

MultiFun Terms: information transfer protein related nucleoproteins, basic proteins
information transfer RNA related Transcription related
regulation type of regulation transcriptional level activator
regulation type of regulation transcriptional level repressor

DNA binding site length: 15 base-pairs

Symmetry: Inverted Repeat

Regulated Transcription Units (95 total): ?

Notes:

Essentiality data for hns knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Pasquali94, Yamada90, Laine84, Kajitani91, Wasinger98, Wilkins98, Link97, UniProt12b]
UniProt: Removed.
Chain 2 -> 137
[UniProt09]
UniProt: DNA-binding protein H-NS;
Mutagenesis-Variant 12
[deAlba11, UniProt14]
Alternate sequence: R → K; UniProt: Abolishes the interaction with Hha.
Amino-Acid-Site 12
[UniProt14]
UniProt: Interacts with Hha; Sequence Annotation Type: site.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
3/2/1998 (pkarp) Merged genes G680/b1237 and EG10457/hns
10/20/97 Gene b1237 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10457; confirmed by SwissProt match.


References

Afflerbach98: Afflerbach H, Schroder O, Wagner R (1998). "Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo." Mol Microbiol 28(3);641-53. PMID: 9632265

Ali99: Ali Azam T, Iwata A, Nishimura A, Ueda S, Ishihama A (1999). "Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid." J Bacteriol 181(20);6361-70. PMID: 10515926

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Azam00: Azam TA, Hiraga S, Ishihama A (2000). "Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid." Genes Cells 5(8);613-26. PMID: 10947847

Azam99: Azam TA, Ishihama A (1999). "Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity." J Biol Chem 274(46);33105-13. PMID: 10551881

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Becker07: Becker NA, Kahn JD, Maher LJ (2007). "Effects of nucleoid proteins on DNA repression loop formation in Escherichia coli." Nucleic Acids Res 35(12);3988-4000. PMID: 17553830

Bertin01: Bertin P, Hommais F, Krin E, Soutourina O, Tendeng C, Derzelle S, Danchin A (2001). "H-NS and H-NS-like proteins in Gram-negative bacteria and their multiple role in the regulation of bacterial metabolism." Biochimie 83(2);235-41. PMID: 11278074

Bertin94: Bertin P, Terao E, Lee EH, Lejeune P, Colson C, Danchin A, Collatz E (1994). "The H-NS protein is involved in the biogenesis of flagella in Escherichia coli." J Bacteriol 1994;176(17);5537-40. PMID: 8071234

Bertin99: Bertin P, Benhabiles N, Krin E, Laurent-Winter C, Tendeng C, Turlin E, Thomas A, Danchin A, Brasseur R (1999). "The structural and functional organization of H-NS-like proteins is evolutionarily conserved in gram-negative bacteria." Mol Microbiol 31(1);319-29. PMID: 9987132

Bloch03: Bloch V, Yang Y, Margeat E, Chavanieu A, Auge MT, Robert B, Arold S, Rimsky S, Kochoyan M (2003). "The H-NS dimerization domain defines a new fold contributing to DNA recognition." Nat Struct Biol 10(3);212-8. PMID: 12592399

Bouvier98: Bouvier J, Gordia S, Kampmann G, Lange R, Hengge-Aronis R, Gutierrez C (1998). "Interplay between global regulators of Escherichia coli: effect of RpoS, Lrp and H-NS on transcription of the gene osmC." Mol Microbiol 1998;28(5);971-80. PMID: 9663683

Brescia03: Brescia CC, Mikulecky PJ, Feig AL, Sledjeski DD (2003). "Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure." RNA 9(1);33-43. PMID: 12554874

Brescia04: Brescia CC, Kaw MK, Sledjeski DD (2004). "The DNA binding protein H-NS binds to and alters the stability of RNA in vitro and in vivo." J Mol Biol 339(3);505-14. PMID: 15147838

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chandraprakash14: Chandraprakash D, Seshasayee AS (2014). "Inhibition of factor-dependent transcription termination in Escherichia coli might relieve xenogene silencing by abrogating H-NS-DNA interactions in vivo." J Biosci 39(1);53-61. PMID: 24499790

Chib12: Chib S, Mahadevan S (2012). "Involvement of the Global Regulator H-NS in the Survival of Escherichia coli in Stationary Phase." J Bacteriol 194(19);5285-93. PMID: 22843842

Corbett07: Corbett D, Bennett HJ, Askar H, Green J, Roberts IS (2007). "SlyA and H-NS regulate transcription of the Escherichia coli K5 capsule gene cluster, and expression of slyA in Escherichia coli is temperature-dependent, positively autoregulated, and independent of H-NS." J Biol Chem 282(46);33326-35. PMID: 17827501

Dame00: Dame RT, Wyman C, Goosen N (2000). "H-NS mediated compaction of DNA visualised by atomic force microscopy." Nucleic Acids Res 28(18);3504-10. PMID: 10982869

Dame05: Dame RT (2005). "The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin." Mol Microbiol 56(4);858-70. PMID: 15853876

De99: De Biase D, Tramonti A, Bossa F, Visca P (1999). "The response to stationary-phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system." Mol Microbiol 32(6);1198-211. PMID: 10383761

deAlba11: de Alba CF, Solorzano C, Paytubi S, Madrid C, Juarez A, Garcia J, Pons M (2011). "Essential residues in the H-NS binding site of Hha, a co-regulator of horizontally acquired genes in Enterobacteria." FEBS Lett 585(12);1765-70. PMID: 21600204

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Donato97: Donato GM, Lelivelt MJ, Kawula TH (1997). "Promoter-specific repression of fimB expression by the Escherichia coli nucleoid-associated protein H-NS." J Bacteriol 179(21);6618-25. PMID: 9352908

Donato99: Donato GM, Kawula TH (1999). "Phenotypic analysis of random hns mutations differentiate DNA-binding activity from properties of fimA promoter inversion modulation and bacterial motility." J Bacteriol 181(3);941-8. PMID: 9922259

Dorman04: Dorman CJ (2004). "H-NS: a universal regulator for a dynamic genome." Nat Rev Microbiol 2(5);391-400. PMID: 15100692

Dorman07: Dorman CJ (2007). "H-NS, the genome sentinel." Nat Rev Microbiol 5(2);157-61. PMID: 17191074

Dorman99: Dorman CJ, Hinton JC, Free A (1999). "Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria." Trends Microbiol 7(3);124-8. PMID: 10203842

Falconi88: Falconi M, Gualtieri MT, La Teana A, Losso MA, Pon CL (1988). "Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS." Mol Microbiol 1988;2(3);323-9. PMID: 3135462

Falconi93: Falconi M, Higgins NP, Spurio R, Pon CL, Gualerzi CO (1993). "Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression." Mol Microbiol 1993;10(2);273-82. PMID: 7934818

Falconi96: Falconi M, Brandi A, La Teana A, Gualerzi CO, Pon CL (1996). "Antagonistic involvement of FIS and H-NS proteins in the transcriptional control of hns expression." Mol Microbiol 19(5);965-75. PMID: 8830277

Fang08: Fang FC, Rimsky S (2008). "New insights into transcriptional regulation by H-NS." Curr Opin Microbiol 11(2);113-20. PMID: 18387844

Forns05: Forns N, Juarez A, Madrid C (2005). "Osmoregulation of the HtrA (DegP) protease of Escherichia coli: an Hha-H-NS complex represses HtrA expression at low osmolarity." FEMS Microbiol Lett 251(1);75-80. PMID: 16143461

Francetic00a: Francetic O, Belin D, Badaut C, Pugsley AP (2000). "Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion." EMBO J 19(24);6697-703. PMID: 11118204

Free95: Free A, Dorman CJ (1995). "Coupling of Escherichia coli hns mRNA levels to DNA synthesis by autoregulation: implications for growth phase control." Mol Microbiol 18(1);101-13. PMID: 8596450

Giangrossi05: Giangrossi M, Zattoni S, Tramonti A, De Biase D, Falconi M (2005). "Antagonistic role of H-NS and GadX in the regulation of the glutamate decarboxylase-dependent acid resistance system in Escherichia coli." J Biol Chem 280(22);21498-505. PMID: 15795232

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Luijsterburg06: Luijsterburg MS, Noom MC, Wuite GJ, Dame RT (2006). "The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: a molecular perspective." J Struct Biol 156(2);262-72. PMID: 16879983

Ma02: Ma Z, Richard H, Tucker DL, Conway T, Foster JW (2002). "Collaborative regulation of Escherichia coli glutamate-dependent acid resistance by two AraC-like regulators, GadX and GadW (YhiW)." J Bacteriol 2002;184(24);7001-12. PMID: 12446650

Madrid07: Madrid C, Balsalobre C, Garcia J, Juarez A (2007). "The novel Hha/YmoA family of nucleoid-associated proteins: use of structural mimicry to modulate the activity of the H-NS family of proteins." Mol Microbiol 63(1);7-14. PMID: 17116239

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May90: May G, Dersch P, Haardt M, Middendorf A, Bremer E (1990). "The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a component of the Escherichia coli K12 nucleoid." Mol Gen Genet 1990;224(1);81-90. PMID: 2177526

McLeod01: McLeod SM, Johnson RC (2001). "Control of transcription by nucleoid proteins." Curr Opin Microbiol 4(2);152-9. PMID: 11282470

Olsen94: Olsen PB, Klemm P (1994). "Localization of promoters in the fim gene cluster and the effect of H-NS on the transcription of fimB and fimE." FEMS Microbiol Lett 1994;116(1);95-100. PMID: 7510658

Olsen98: Olsen PB, Schembri MA, Gally DL, Klemm P (1998). "Differential temperature modulation by H-NS of the fimB and fimE recombinase genes which control the orientation of the type 1 fimbrial phase switch." FEMS Microbiol Lett 1998;162(1);17-23. PMID: 9595659

Oshima06: Oshima T, Ishikawa S, Kurokawa K, Aiba H, Ogasawara N (2006). "Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase." DNA Res 13(4);141-53. PMID: 17046956

Panyukov13: Panyukov VV, Ozoline ON (2013). "Promoters of Escherichia coli versus promoter islands: function and structure comparison." PLoS One 8(5);e62601. PMID: 23717391

Pasquali94: Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. (1994). Data submission to UniProtKB on 1994-09.

Paytubi04: Paytubi S, Madrid C, Forns N, Nieto JM, Balsalobre C, Uhlin BE, Juarez A (2004). "YdgT, the Hha paralogue in Escherichia coli, forms heteromeric complexes with H-NS and StpA." Mol Microbiol 54(1);251-63. PMID: 15458420

Pon88: Pon CL, Calogero RA, Gualerzi CO (1988). "Identification, cloning, nucleotide sequence and chromosomal map location of hns, the structural gene for Escherichia coli DNA-binding protein H-NS." Mol Gen Genet 1988;212(2);199-202. PMID: 2841565

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Ussery94: Ussery DW, Hinton JC, Jordi BJ, Granum PE, Seirafi A, Stephen RJ, Tupper AE, Berridge G, Sidebotham JM, Higgins CF (1994). "The chromatin-associated protein H-NS." Biochimie 1994;76(10-11);968-80. PMID: 7748941

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Other References Related to Gene Regulation

Brandi94: Brandi A, Pon CL, Gualerzi CO (1994). "Interaction of the main cold shock protein CS7.4 (CspA) of Escherichia coli with the promoter region of hns." Biochimie 1994;76(10-11);1090-8. PMID: 7748932

Dersch93: Dersch P, Schmidt K, Bremer E (1993). "Synthesis of the Escherichia coli K-12 nucleoid-associated DNA-binding protein H-NS is subjected to growth-phase control and autoregulation." Mol Microbiol 1993;8(5);875-89. PMID: 8355613

Giangrossi01: Giangrossi M, Gualerzi CO, Pon CL (2001). "Mutagenesis of the downstream region of the Escherichia coli hns promoter." Biochimie 83(2);251-9. PMID: 11278076

Hommais04: Hommais F, Krin E, Coppee JY, Lacroix C, Yeramian E, Danchin A, Bertin P (2004). "GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli." Microbiology 150(Pt 1);61-72. PMID: 14702398

La89: La Teana A, Falconi M, Scarlato V, Lammi M, Pon CL (1989). "Characterization of the structural genes for the DNA-binding protein H-NS in Enterobacteriaceae." FEBS Lett 1989;244(1);34-8. PMID: 2494066

La91: La Teana A, Brandi A, Falconi M, Spurio R, Pon CL, Gualerzi CO (1991). "Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS." Proc Natl Acad Sci U S A 1991;88(23);10907-11. PMID: 1961761

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

Oberto10: Oberto J (2010). "FITBAR: a web tool for the robust prediction of prokaryotic regulons." BMC Bioinformatics 11;554. PMID: 21070640


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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