Bacterial DNA binding protein

Last updated
Bac_DNA_binding
PDB 1p51 EBI.jpg
anabaena hu-dna cocrystal structure (ahu6)
Identifiers
SymbolBac_DNA_binding
Pfam PF00216
InterPro IPR000119
PROSITE PDOC00044
SCOP2 1hue / SCOPe / SUPFAM
CDD cd00591
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In molecular biology, bacterial DNA binding proteins are a family of small, usually basic proteins of about 90 residues that bind DNA and are known as histone-like proteins. [1] [2] Since bacterial binding proteins have a diversity of functions, it has been difficult to develop a common function for all of them. They are commonly referred to as histone-like and have many similar traits with the eukaryotic histone proteins. Eukaryotic histones package DNA to help it to fit in the nucleus, and they are known to be the most conserved proteins in nature. [3] Examples include the HU protein in Escherichia coli , a dimer of closely related alpha and beta chains and in other bacteria can be a dimer of identical chains. HU-type proteins have been found in a variety of bacteria (including cyanobacteria) and archaea, and are also encoded in the chloroplast genome of some algae. [4] The integration host factor (IHF), a dimer of closely related chains which is suggested to function in genetic recombination as well as in translational and transcriptional control [5] is found in Enterobacteria and viral proteins including the African swine fever virus protein A104R (or LMW5-AR). [6]

Contents

This family is also found in a group of eukaryotes known as dinoflagellates. These dinoflagellate histone-like proteins replace histone in some dinoflagellates and package DNA into a liquid-crystalline state. [7]

History

Histone-like proteins are present in many Eubacteria, Cyanobacteria, and Archaebacteria. These proteins participate in all DNA-dependent functions; in these processes, bacterial DNA binding proteins have an architectural role, maintaining structural integrity as transcription, recombination, replication, or any other DNA-dependent process proceeds. Eukaryotic histones were first discovered through experiments in 0.4M NaCl. In these high salt concentrations, the eukaryotic histone protein is eluted from a DNA solution in which single stranded DNA is bound covalently to cellulose. Following elution, the protein readily binds DNA, indicating the protein's high affinity for DNA. Histone-like proteins were unknown to be present in bacteria until similarities between eukaryotic histones and the HU-protein were noted, particularly because of the abundancy, basicity, and small size of both of the proteins. [8] Upon further investigation, it was discovered that the amino acid composition of HU resembles that of eukaryotic histones, thus prompting further research into the exact function of bacterial DNA binding proteins and discoveries of other related proteins in bacteria.

Role in DNA replication

Research suggests that bacterial DNA binding protein has an important role during DNA replication; the protein is involved in stabilizing the lagging strand as well as interacting with DNA polymerase III. The role of single-stranded DNA binding (SSB) protein during DNA replication in Escherichia coli cells has been studied, specifically the interactions between SSB and the χ subunit of DNA polymerase III in environments of varying salt concentrations. [9]

In DNA replication at the lagging strand site, DNA polymerase III removes nucleotides individually from the DNA binding protein. An unstable SSB/DNA system would result in rapid disintegration of the SSB, which stalls DNA replication. Research has shown that the ssDNA is stabilized by the interaction of SSB and the χ subunit of DNA polymerase III in E. coli, thus preparing for replication by maintaining the correct conformation that increases the binding affinity of enzymes to ssDNA. Furthermore, binding of SSB to DNA polymerase III at the replication fork prevents dissociation of SSB, consequently increasing the efficiency of DNA polymerase III to synthesize a new DNA strand.

Examples

H-NS

(i) RNA polymerase at the promoter is surrounded by curved DNA. (ii) This curved DNA wraps around the polymerase. (iii) H-NS binds to the curved DNA to lock the RNA polymerase at the promoter and prevents transcription from occurring. (iv) Environmental signals and transcription factors release the DNA bacterial binding protein and allows transcription to proceed. H-NS.jpg
(i) RNA polymerase at the promoter is surrounded by curved DNA. (ii) This curved DNA wraps around the polymerase. (iii) H-NS binds to the curved DNA to lock the RNA polymerase at the promoter and prevents transcription from occurring. (iv) Environmental signals and transcription factors release the DNA bacterial binding protein and allows transcription to proceed.

Initially, bacterial DNA binding proteins were thought to help stabilize bacterial DNA. Currently, many more functions of bacteria DNA binding proteins have been discovered, including the regulation of gene expression by histone-like nucleoid-structuring protein, H-NS.

H-NS is about 15.6 kDa and assists in the regulation of bacterial transcription in bacteria by repressing and activating certain genes. H-NS binds to DNA with an intrinsic curvature. In E. coli, H-NS binds to a P1 promoter decreasing rRNA production during stationary and slow growth periods. RNA polymerase and H-NS DNA binding protein have overlapping binding sites; it is thought that H-NS regulates rRNA production by acting on the transcription initiation site. It has been found that H-NS and RNA polymerase both bind to the P1 promoter and form a complex. When H-NS is bound with RNA Polymerase to the promoter region, there are structural differences in the DNA that are accessible. [11] It has also been found that H-NS can affect translation as well by binding to mRNA and causing its degradation.

HU

HU is a small (10 kDa [12] ) bacterial DNA-binding protein, which structurally differs from a eukaryotic histone but functionally acts similarly to a histone by inducing negative supercoiling into circular DNA with the assistance of topoisomerase. The protein has been implicated in DNA replication, recombination, and repair. With an α-helical hydrophobic core and two positively charged β-ribbon arms, HU binds non-specifically to dsDNA with low affinity but binds to altered DNA—such as junctions, nicks, gaps, forks, and overhangs—with high affinity. The arms bind to the minor groove of DNA in low affinity states; in high affinity states, a component of the α-helical core interacts with the DNA as well. However, this protein's function is not solely confined to DNA; HU also binds to RNA and DNA-RNA hybrids with the same affinity as supercoiled DNA. [13]

Recent research has revealed that HU binds with high specificity to the mRNA of rpoS, [14] a transcript for the stress sigma factor of RNA polymerase, and stimulates translation of the protein. Additional to this RNA function, it was also demonstrated that HU binds DsrA, a small non-coding RNA that regulates transcription through repressing H-NS and stimulates translation through increasing expression of rpoS. These interactions suggest that HU has multiple influences on transcription and translation in bacterial cells.

IHF

Integration host factor, IHF, is not a nucleoid-associated protein only found in gram negative bacteria. [15] It is a 20 kDa heterodimer, composed of α and β subunits that bind to the sequence 5' - WATCAANNNNTTR - 3' and bends the DNA approximately 160 degrees. [16] The β arms of IHF have Proline residues that help stabilize the DNA kinks. These kinks can help compact DNA and allow for supercoiling. The mode of binding to DNA depends on environmental factors, such as the concentration of ions present. With a high concentration of KCl, there is weak DNA bending. It has been found that sharper DNA bending occurs when the concentration of KCl is less than 100 mM, and IHF is not concentrated. [17]

IHF was discovered as a necessary co-factor for recombination of λ phage into E.coli. In 2016 it was discovered that IHF also plays a key role in CRISPR type I and type II systems. It has a major role in allowing the Cas1-Cas2 complex to integrate new spacers into the CRISPR sequence. The bending of the DNA by IHF is thought to alter spacing in the DNA major and minor grooves, allowing the Cas1-Cas2 complex to make contact with the DNA bases. [18] This is a key function in the CRISPR system as it ensures that new spacers area always added at the beginning of the CRISPR sequence next to the leader sequence. This directing of integration by IHF ensures that spacers are added chronologically, allowing better protection against the most recent viral infection. [19]

Comparison

Table 1. Comparison of some DNA Binding Proteins
DNA Binding ProteinSizeStructureBinding SiteEffect
H-NS15.6 kDaexists in dimers to physically prevent RNA polymerase from binding to promoterbinds to bent DNA, binds to P1 promoter in E. coliregulation of gene expression
HU10 kDaα-helical core and two positively charged β-ribbon armsbinds non-specifically to dsDNA, binds to DsrA, a small non-coding RNA that regulates transcriptioninduces negative supercoiling into circular DNA
IHF22 kDaαβαβ hetrodimerbinds to specific sequences of DNAcreates kinks in DNA

Implications and further research

The functions of bacterial DNA-binding proteins are not limited to DNA replication. Researchers have been investigating other pathways these proteins affect. The DNA-binding protein H-NS has been known to play roles in chromosome organization and gene regulation; however, recent studies have also confirmed their role in indirectly regulating flagella functions. [20] Some motility regulatory linkages that H-NS influences include the messenger molecule Cyclic di-GMP, the bio-film regulatory protein CsgD, and the sigma factors, σ(S) and σ(F). Further studies are aiming to characterize the ways this nucleoid-organizing protein affects the motility of the cell through other regulatory pathways.

Other researchers have used bacterial DNA-binding proteins to research Salmonella enterica serovar Typhimurium, in which the T6SS genes are activated from a macrophage infection. When S. Typhimurium infects, their efficiency can be improved through a sense-and-kill mechanism with T6SS H-NS silencing. [21] Assays are created that combine reporter fusions, electrophoretic mobility shift assays, DNase footprinting, and fluorescence microscopy to silence the T6SS gene cluster by the histone-like nucleoid structuring H-NS protein.

See also

Related Research Articles

<span class="mw-page-title-main">DNA replication</span> Biological process

In molecular biology, DNA replication is the biological process of producing two identical replicas of DNA from one original DNA molecule. DNA replication occurs in all living organisms acting as the most essential part of biological inheritance. This is essential for cell division during growth and repair of damaged tissues, while it also ensures that each of the new cells receives its own copy of the DNA. The cell possesses the distinctive property of division, which makes replication of DNA essential.

<span class="mw-page-title-main">Lambda phage</span> Bacteriophage that infects Escherichia coli

Enterobacteria phage λ is a bacterial virus, or bacteriophage, that infects the bacterial species Escherichia coli. It was discovered by Esther Lederberg in 1950. The wild type of this virus has a temperate life cycle that allows it to either reside within the genome of its host through lysogeny or enter into a lytic phase, during which it kills and lyses the cell to produce offspring. Lambda strains, mutated at specific sites, are unable to lysogenize cells; instead, they grow and enter the lytic cycle after superinfecting an already lysogenized cell.

<span class="mw-page-title-main">Transcription (biology)</span> Process of copying a segment of DNA into RNA

Transcription is the process of copying a segment of DNA into RNA. The segments of DNA transcribed into RNA molecules that can encode proteins are said to produce messenger RNA (mRNA). Other segments of DNA are copied into RNA molecules called non-coding RNAs (ncRNAs). mRNA comprises only 1–3% of total RNA samples. Less than 2% of the human genome can be transcribed into mRNA, while at least 80% of mammalian genomic DNA can be actively transcribed, with the majority of this 80% considered to be ncRNA.

<span class="mw-page-title-main">RNA polymerase</span> Enzyme that synthesizes RNA from DNA

In molecular biology, RNA polymerase, or more specifically DNA-directed/dependent RNA polymerase (DdRP), is an enzyme that catalyzes the chemical reactions that synthesize RNA from a DNA template.

In molecular biology and genetics, transcriptional regulation is the means by which a cell regulates the conversion of DNA to RNA (transcription), thereby orchestrating gene activity. A single gene can be regulated in a range of ways, from altering the number of copies of RNA that are transcribed, to the temporal control of when the gene is transcribed. This control allows the cell or organism to respond to a variety of intra- and extracellular signals and thus mount a response. Some examples of this include producing the mRNA that encode enzymes to adapt to a change in a food source, producing the gene products involved in cell cycle specific activities, and producing the gene products responsible for cellular differentiation in multicellular eukaryotes, as studied in evolutionary developmental biology.

<span class="mw-page-title-main">Rho factor</span> Prokaryotic protein

A ρ factor is a bacterial protein involved in the termination of transcription. Rho factor binds to the transcription terminator pause site, an exposed region of single stranded RNA after the open reading frame at C-rich/G-poor sequences that lack obvious secondary structure.

A sigma factor is a protein needed for initiation of transcription in bacteria. It is a bacterial transcription initiation factor that enables specific binding of RNA polymerase (RNAP) to gene promoters. It is homologous to archaeal transcription factor B and to eukaryotic factor TFIIB. The specific sigma factor used to initiate transcription of a given gene will vary, depending on the gene and on the environmental signals needed to initiate transcription of that gene. Selection of promoters by RNA polymerase is dependent on the sigma factor that associates with it. They are also found in plant chloroplasts as a part of the bacteria-like plastid-encoded polymerase (PEP).

A transcriptional activator is a protein that increases transcription of a gene or set of genes. Activators are considered to have positive control over gene expression, as they function to promote gene transcription and, in some cases, are required for the transcription of genes to occur. Most activators are DNA-binding proteins that bind to enhancers or promoter-proximal elements. The DNA site bound by the activator is referred to as an "activator-binding site". The part of the activator that makes protein–protein interactions with the general transcription machinery is referred to as an "activating region" or "activation domain".

<span class="mw-page-title-main">Nucleoid</span> Region within a prokaryotic cell containing genetic material

The nucleoid is an irregularly shaped region within the prokaryotic cell that contains all or most of the genetic material. The chromosome of a typical prokaryote is circular, and its length is very large compared to the cell dimensions, so it needs to be compacted in order to fit. In contrast to the nucleus of a eukaryotic cell, it is not surrounded by a nuclear membrane. Instead, the nucleoid forms by condensation and functional arrangement with the help of chromosomal architectural proteins and RNA molecules as well as DNA supercoiling. The length of a genome widely varies and a cell may contain multiple copies of it.

<span class="mw-page-title-main">DNA-binding protein</span> Proteins that bind with DNA, such as transcription factors, polymerases, nucleases and histones

DNA-binding proteins are proteins that have DNA-binding domains and thus have a specific or general affinity for single- or double-stranded DNA. Sequence-specific DNA-binding proteins generally interact with the major groove of B-DNA, because it exposes more functional groups that identify a base pair.

<span class="mw-page-title-main">General transcription factor</span> Class of protein transcription factors

General transcription factors (GTFs), also known as basal transcriptional factors, are a class of protein transcription factors that bind to specific sites (promoter) on DNA to activate transcription of genetic information from DNA to messenger RNA. GTFs, RNA polymerase, and the mediator constitute the basic transcriptional apparatus that first bind to the promoter, then start transcription. GTFs are also intimately involved in the process of gene regulation, and most are required for life.

In molecular biology, a termination factor is a protein that mediates the termination of RNA transcription by recognizing a transcription terminator and causing the release of the newly made mRNA. This is part of the process that regulates the transcription of RNA to preserve gene expression integrity and are present in both eukaryotes and prokaryotes, although the process in bacteria is more widely understood. The most extensively studied and detailed transcriptional termination factor is the Rho (ρ) protein of E. coli.

<span class="mw-page-title-main">Replisome</span> Molecular complex

The replisome is a complex molecular machine that carries out replication of DNA. The replisome first unwinds double stranded DNA into two single strands. For each of the resulting single strands, a new complementary sequence of DNA is synthesized. The total result is formation of two new double stranded DNA sequences that are exact copies of the original double stranded DNA sequence.

<span class="mw-page-title-main">Prokaryotic DNA replication</span> DNA Replication in prokaryotes

Prokaryotic DNA Replication is the process by which a prokaryote duplicates its DNA into another copy that is passed on to daughter cells. Although it is often studied in the model organism E. coli, other bacteria show many similarities. Replication is bi-directional and originates at a single origin of replication (OriC). It consists of three steps: Initiation, elongation, and termination.

<span class="mw-page-title-main">Eukaryotic transcription</span> Transcription is heterocatalytic function of DNA

Eukaryotic transcription is the elaborate process that eukaryotic cells use to copy genetic information stored in DNA into units of transportable complementary RNA replica. Gene transcription occurs in both eukaryotic and prokaryotic cells. Unlike prokaryotic RNA polymerase that initiates the transcription of all different types of RNA, RNA polymerase in eukaryotes comes in three variations, each translating a different type of gene. A eukaryotic cell has a nucleus that separates the processes of transcription and translation. Eukaryotic transcription occurs within the nucleus where DNA is packaged into nucleosomes and higher order chromatin structures. The complexity of the eukaryotic genome necessitates a great variety and complexity of gene expression control.

fis E. coli gene

fis is an E. coli gene encoding the Fis protein. The regulation of this gene is more complex than most other genes in the E. coli genome, as Fis is an important protein which regulates expression of other genes. It is supposed that fis is regulated by H-NS, IHF and CRP. It also regulates its own expression (autoregulation). Fis is one of the most abundant DNA binding proteins in Escherichia coli under nutrient-rich growth conditions.

RNA polymerase II holoenzyme is a form of eukaryotic RNA polymerase II that is recruited to the promoters of protein-coding genes in living cells. It consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins.

<span class="mw-page-title-main">Bacterial one-hybrid system</span> Method for identifying the sequence-specific target site of a DNA-binding domain

The bacterial one-hybrid (B1H) system is a method for identifying the sequence-specific target site of a DNA-binding domain. In this system, a given transcription factor (TF) is expressed as a fusion to a subunit of RNA polymerase. In parallel, a library of randomized oligonucleotides representing potential TF target sequences are cloned into a separate vector containing the selectable genes HIS3 and URA3. If the DNA-binding domain (bait) binds a potential DNA target site (prey) in vivo, it will recruit RNA polymerase to the promoter and activate transcription of the reporter genes in that clone. The two reporter genes, HIS3 and URA3, allow for positive and negative selections, respectively. At the end of the process, positive clones are sequenced and examined with motif-finding tools in order to resolve the favoured DNA target sequence.

<span class="mw-page-title-main">Histone-like nucleoid-structuring protein</span>

Histone-like nucleoid-structuring protein (H-NS), is one of twelve nucleoid-associated proteins (NAPs) whose main function is the organization of genetic material, including the regulation of gene expression via xenogeneic silencing. H-NS is characterized by an N-terminal domain (NTD) consisting of two dimerization sites, a linker region that is unstructured and a C-terminal domain (CTD) that is responsible for DNA-binding. Though it is a small protein, it provides essential nucleoid compaction and regulation of genes and is highly expressed, functioning as a dimer or multimer. Change in temperature causes H-NS to be dissociated from the DNA duplex, allowing for transcription by RNA polymerase, and in specific regions lead to pathogenic cascades in enterobacteria such as Escherichia coli and the four Shigella species.

The locus of enterocyte effacement-encoded regulator (Ler) is a regulatory protein that controls bacterial pathogenicity of enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic Escherichia coli (EHEC). More specifically, Ler regulates the locus of enterocyte effacement (LEE) pathogenicity island genes, which are responsible for creating intestinal attachment and effacing lesions and subsequent diarrhea: LEE1, LEE2, and LEE3. LEE1, 2, and 3 carry the information necessary for a type III secretion system. The transcript encoding the Ler protein is the open reading frame 1 on the LEE1 operon.

References

  1. ↑ Drlica K, Rouviere-Yaniv J (September 1987). "Histonelike proteins of bacteria". Microbiological Reviews. 51 (3): 301–19. doi:10.1128/MMBR.51.3.301-319.1987. PMC   373113 . PMID   3118156.
  2. ↑ Pettijohn DE (September 1988). "Histone-like proteins and bacterial chromosome structure". The Journal of Biological Chemistry. 263 (26): 12793–6. doi: 10.1016/S0021-9258(18)37625-7 . PMID   3047111.
  3. ↑ Griffiths, Anthony; Wessler, Susan; Carroll, Sean; Doebly, John. Introduction to Genetic Analysis (10 ed.). New York: W. H. Freeman and Company. pp. 428–429.
  4. ↑ Wang SL, Liu XQ (December 1991). "The plastid genome of Cryptomonas phi encodes an hsp70-like protein, a histone-like protein, and an acyl carrier protein". Proceedings of the National Academy of Sciences of the United States of America. 88 (23): 10783–7. Bibcode:1991PNAS...8810783W. doi: 10.1073/pnas.88.23.10783 . PMC   53015 . PMID   1961745.
  5. ↑ Friedman DI (November 1988). "Integration host factor: a protein for all reasons" (PDF). Cell. 55 (4): 545–54. doi:10.1016/0092-8674(88)90213-9. hdl: 2027.42/27063 . PMID   2972385. S2CID   8548040.
  6. ↑ Neilan JG, Lu Z, Kutish GF, Sussman MD, Roberts PC, Yozawa T, Rock DL (March 1993). "An African swine fever virus gene with similarity to bacterial DNA binding proteins, bacterial integration host factors, and the Bacillus phage SPO1 transcription factor, TF1". Nucleic Acids Research. 21 (6): 1496. doi:10.1093/nar/21.6.1496. PMC   309344 . PMID   8464748.
  7. ↑ Riaz, S; Sui, Z; Niaz, Z; Khan, S; Liu, Y; Liu, H (14 December 2018). "Distinctive Nuclear Features of Dinoflagellates with A Particular Focus on Histone and Histone-Replacement Proteins". Microorganisms. 6 (4): 128. doi: 10.3390/microorganisms6040128 . PMC   6313786 . PMID   30558155.
  8. ↑ Drlica K, Rouviere-Yaniv J (September 1987). "Histonelike proteins of bacteria". Microbiological Reviews. 51 (3): 301–19. doi:10.1128/MMBR.51.3.301-319.1987. PMC   373113 . PMID   3118156.
  9. ↑ Witte G, Urbanke C, Curth U (August 2003). "DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery". Nucleic Acids Research. 31 (15): 4434–40. doi:10.1093/nar/gkg498. PMC   169888 . PMID   12888503.
  10. ↑ Dorman, Charles J; Deighan, Padraig (2003-04-01). "Regulation of gene expression by histone-like proteins in bacteria". Current Opinion in Genetics & Development. 13 (2): 179–184. doi:10.1016/S0959-437X(03)00025-X. PMID   12672495.
  11. ↑ Schröder O, Wagner R (May 2000). "The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex". Journal of Molecular Biology. 298 (5): 737–48. doi:10.1006/jmbi.2000.3708. PMID   10801345.
  12. ↑ Serban D, Arcineigas SF, Vorgias CE, Thomas GJ (April 2003). "Structure and dynamics of the DNA-binding protein HU of B. stearothermophilus investigated by Raman and ultraviolet-resonance Raman spectroscopy". Protein Science. 12 (4): 861–70. doi:10.1110/ps.0234103. PMC   2323852 . PMID   12649443.
  13. ↑ Balandina A, Kamashev D, Rouviere-Yaniv J (August 2002). "The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids". The Journal of Biological Chemistry. 277 (31): 27622–8. doi: 10.1074/jbc.M201978200 . PMID   12006568.
  14. ↑ Balandina A, Claret L, Hengge-Aronis R, Rouviere-Yaniv J (February 2001). "The Escherichia coli histone-like protein HU regulates rpoS translation". Molecular Microbiology. 39 (4): 1069–79. doi: 10.1046/j.1365-2958.2001.02305.x . PMID   11251825.
  15. ↑ Dillon SC, Dorman CJ (March 2010). "Bacterial nucleoid-associated proteins, nucleoid structure and gene expression". Nature Reviews. Microbiology. 8 (3): 185–95. doi:10.1038/nrmicro2261. PMID   20140026. S2CID   33103160.
  16. ↑ Nuñez JK, Bai L, Harrington LB, Hinder TL, Doudna JA (June 2016). "CRISPR Immunological Memory Requires a Host Factor for Specificity". Molecular Cell. 62 (6): 824–833. doi: 10.1016/j.molcel.2016.04.027 . PMID   27211867.
  17. ↑ Lin J, Chen H, Dröge P, Yan J (2012). "Physical organization of DNA by multiple non-specific DNA-binding modes of integration host factor (IHF)". PLOS ONE. 7 (11): e49885. Bibcode:2012PLoSO...749885L. doi: 10.1371/journal.pone.0049885 . PMC   3498176 . PMID   23166787.
  18. ↑ Nuñez JK, Bai L, Harrington LB, Hinder TL, Doudna JA (June 2016). "CRISPR Immunological Memory Requires a Host Factor for Specificity". Molecular Cell. 62 (6): 824–833. doi: 10.1016/j.molcel.2016.04.027 . PMID   27211867.
  19. ↑ Sorek R, Lawrence CM, Wiedenheft B (2013). "CRISPR-mediated adaptive immune systems in bacteria and archaea". Annual Review of Biochemistry. 82 (1): 237–66. doi:10.1146/annurev-biochem-072911-172315. PMID   23495939.
  20. ↑ Kim EA, Blair DF (October 2015). "Function of the Histone-Like Protein H-NS in Motility of Escherichia coli: Multiple Regulatory Roles Rather than Direct Action at the Flagellar Motor". Journal of Bacteriology. 197 (19): 3110–20. doi:10.1128/JB.00309-15. PMC   4560294 . PMID   26195595.
  21. ↑ Brunet YR, Khodr A, Logger L, Aussel L, Mignot T, Rimsky S, Cascales E (July 2015). "H-NS Silencing of the Salmonella Pathogenicity Island 6-Encoded Type VI Secretion System Limits Salmonella enterica Serovar Typhimurium Interbacterial Killing". Infection and Immunity. 83 (7): 2738–50. doi:10.1128/IAI.00198-15. PMC   4468533 . PMID   25916986.
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