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  4. Recombinant Escherichia coli DNA-binding protein H-NS (hns)

Recombinant Escherichia coli DNA-binding protein H-NS (hns)

In Stock
  • 货号：
    CSB-EP359764ENV
  • 规格：
    ￥2328
  • 图片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

产品详情

  • 纯度：
    Greater than 85% as determined by SDS-PAGE.
  • 基因名：
    hns
  • Uniprot No.：
  • 别名：
    hns; bglY; cur; drdX; hnsA; msyA; osmZ; pilG; topS; b1237; JW1225; DNA-binding protein H-NS; Heat-stable nucleoid-structuring protein; Histone-like protein HLP-II; Protein B1; Protein H1
  • 种属：
    Escherichia coli (strain K12)
  • 蛋白长度：
    Full Length of Mature Protein
  • 来源：
    E.coli
  • 分子量：
    19.5 kDa
  • 表达区域：
    2-137aa
  • 氨基酸序列
    SEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSLAAVKSGTKAKRAQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ
    Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
  • 蛋白标签：
    N-terminal 6xHis-tagged
  • 产品提供形式：
    Liquid or Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 缓冲液：
    Tris-based buffer，50% glycerol
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期：
    3-7 business days
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet & COA：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    A DNA-binding protein implicated in transcriptional repression (silencing). Also involved in bacterial chromosome organization and compaction. H-NS binds tightly to AT-rich dsDNA and inhibits transcription. Binds upstream and downstream of initiating RNA polymerase, trapping it in a loop and preventing transcription. Binds to hundreds of sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome. 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. Suppresses transcription at many intragenic sites as well as transcription of spurious, non-coding RNAs genome-wide. 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. 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. The protein forms 2 clusters in the nucleoid which gather hns-bound loci together, bridging non-contiguous DNA, and causes DNA substantial condensation. 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. Transcriptional repression can be inhibited by dominant-negative mutants of StpA or itself. May effect transcriptional elongation. Can increase translational efficiency of mRNA with suboptimal Shine-Dalgarno sequences. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Plays a role in flagellar function. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its repression is antagonized by LeuO. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150. Overexpression suppresses secY24, a temperature-sensitive mutation. Has also been reported to activate transcription of some genes.
  • 基因功能参考文献：
    1. H-NS specifically represses LEE5 promoter activity and Ler alleviates the repression by H-NS. PMID: 28013045
    2. Transcription and stability of cas3 in Deltahns cells is limiting for resistance to phage. PMID: 26956996
    3. we propose that, during E. coli evolution, the conservation of H-NS binding sites resulted in the diversification of the regulation of horizontally transferred genes, which may have facilitated E. coli adaptation to new ecological niches PMID: 26789284
    4. Through DNA binding, the two proteins interplay to form a transient ternary complex Fpg/DNA/HU which results in the release of Fpg and the molecular entrapment of SSBs by HU PMID: 26392572
    5. The fdeC gene encodes a protein that is expressed at the cell surface and promotes biofilm formation under continuous-flow conditions and is repressed by the global regulator H-NS. PMID: 25239893
    6. It was concluded that H-NS exerts maximum repression of LEE5 via the specific sequence at around -138 and subsequently contacts a subunit of RNAP through oligomerization. PMID: 24610333
    7. Bicyclomycin treatment leads to a decrease in binding signal for H-NS to the E. coli chromosome. PMID: 24499790
    8. Both the DNA binding sites of H-NS as well as the function of StpA as a backup system might be selected for silencing highly transcribable genes. PMID: 23661089
    9. We show that H-NS modulates the expression of the nrdAB and nrdDG operons in aerobically and in anaerobically growing cells. PMID: 23873909
    10. H-NS represses LEE5p by binding to a cluster of A tracks upstream of -114 of the promoter. PMID: 22924981
    11. RcsB-BglJ activates one of two H-NS-StpA repressed leuO promoters. PMID: 22295907
    12. The product of bacreriophage T7 gene 5.5 (gp5.5) forms a stable complex with the Escherichia coli histone-like protein H-NS and transfer RNAs (tRNAs). PMID: 22566619
    13. the attractive force that governs the Cnu-H-NS interaction is an ionic bond, unlike the hydrophobic interaction that is the major attractive force in most proteins. PMID: 22358512
    14. HNS control the integrase IntI1 and integron promoters expression. PMID: 21778209
    15. LeuO is a major player in antagonistic interplay against the universal silencer H-NS. PMID: 21883529
    16. It binds to a middle domain of FliG that bridges the core parts of the rotor and parts nearer the edge that interact with the stator. PMID: 21890701
    17. Rho-dependent transcription termination is regulated by the H-NS family of proteins. PMID: 21602341
    18. Combinations of the rho, nusG, and nusA mutations were synthetically lethal, and the lethality was suppressed by expression of H-NS. PMID: 21602355
    19. a new insight into the bolA regulation network demonstrating that H-NS represses the transcription of this important gene was provided. PMID: 21708124
    20. H-NS formed 2 compact clusters per chromosome, driven by oligomerization of DNA-bound H-NS through interactions mediated by the amino-terminal domain of the protein; observations demonstrate H-NS plays a key role in global chromosome organization PMID: 21903814
    21. Chromosomal and plasmidencoded H-NS proteins differ in their functional properties. PMID: 21320594
    22. H-NS binds to long tracts of DNA, consistent with the linear spread of H-NS binding from high- to surrounding lower-affinity sites; the length of binding regions is associated with the degree of transcriptional repression imposed by H-NS. PMID: 21097887
    23. H-NS directly controls regulators of stress resistance. PMID: 21034467
    24. H-NS and LeuO are antagonistic regulators of CRISPR-based immunity. PMID: 20659289
    25. The global regulator H-NS is required for e xtracellular DNA (eDNA) production since DNA was not detected for the hns mutant and production of H-NS restored eDNA production to wild-type levels. PMID: 20833130
    26. findings substantiate the central role of RcsB in H-NS-mediated control of motility and acid stress resistance PMID: 20435136
    27. These results demonstrate an active involvement of H-NS in the induction of the CRISPR-cas system and suggest a potential link between two prokaryotic defence systems against foreign DNA. PMID: 20132443
    28. Binding of the IHF protein to a site immediately adjacent to fimS is required for phase-on orientational bias; in the absence of LRP and IHF binding, fimS adopts the off orientation and the H-NS protein is required to maintain this orientational bias. PMID: 19889099
    29. protein-induced DNA bending plays an important role in HU site-specific DNA binding and supports a model of a mutually induced fit. PMID: 15322284
    30. forms complexes with with YdgT in vivo PMID: 15458420
    31. data show that the H-NS acts to repress the expression of traM and traJ as cells enter stationary phase, thereby decreasing mating ability to barely detectable levels PMID: 15491366
    32. Analysis of mechanical response generated by binding of DNA-bending protein Hu to single tethered 48.5 kb lambda-DNA molecules finds that compaction of DNA increases with increasing Hu concentration. PMID: 15504049
    33. key role for intrinsic conformational changes of Hha in modulating its interaction with H-NS PMID: 15720293
    34. H-NS directly inhibits gadA and gadX transcription and, by controlling the intracellular level of the activator GadX, indirectly affects the expression of the whole gad system PMID: 15795232
    35. the expression of the H-NS regulon is sensitive to small changes in the cellular level of H-NS, enabling the cell to response rapidly to environment cues PMID: 15819627
    36. Results show that LRP binds to the regulatory region of bacterial rRNA promoters, and may contribute in combination with H-NS to the control of rRNA synthesis. PMID: 16238633
    37. The oligomerization capacity of H-NS in vivo is effected by temperature, pH, and osmolarity. PMID: 16303134
    38. StpA complements H-NS proteins defective in DNA binding to repress bgl, while in autoregulation of stpA it acts autonomously, indicating a difference in the mechanisms of repression. PMID: 16980475
    39. role of hns in regulation of RpoS; findings suggest that H-NS regulates an RssB inhibitor or inhibitors PMID: 16980505
    40. The results support the conclusion that the bacterial DNA-binding protein LRP, assisted by H-NS, forms a repressive nucleoprotein structure involved in regulation of rRNA transcription. PMID: 17196617
    41. Identified as new member of the polyamine modulon together with RpoN and Cra. PMID: 17220219
    42. crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein PMID: 17360520
    43. The binding of H-NS to a transposase protein is a novel function for this important regulatory molecule. PMID: 17501923
    44. analysis of H-NS repression by binding within the transcription unit PMID: 17569663
    45. Data Show that H-NS prevented binding of RNA polymerase (RNAP) at the Hemolysin Protein E promoter (PhlyE). PMID: 17892462
    46. The model for the functions of H-NS in homologous recombination and double-strand break repair is discussed PMID: 17991999
    47. LeuO and H-NS regulate the expression of the yjjQ-bglJ operon and yjjP. PMID: 18055596
    48. H-NS is shown to be a common regulator of multiple iron and other nutrient acquisition systems preferentially expressed at 37 degrees C and of general stress response, biofilm formation, and cold shock genes highly expressed at 23 degrees C. PMID: 19011022
    49. At 37 degrees C, SlyA activates transcription of K5 capsule independent of H-NS but maximal transcription requires H-NS. PMID: 19114478
    50. StpA binding profile reduced to one-third in the hns mutant and the H-NS binding profile was unaffected by stpA inactivation. PMID: 19151137

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  • 亚细胞定位：
    Cytoplasm, nucleoid.
  • 蛋白家族：
    Histone-like protein H-NS family
  • 数据库链接：

    KEGG: ecj:JW1225

    STRING: 316385.ECDH10B_1297