Key Points
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Nucleoid-associated proteins in bacteria perform roles that influence all of the major DNA transactions.
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In Escherichia coli and other Gram-negative bacteria, the H-NS nucleoid-associated protein has a global and negative influence on gene expression. Detailed information is emerging about the mechanisms by which H-NS exerts its negative effects.
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Knowledge of the domain structure of the H-NS protein is central to the understanding of its biological role. It is becoming clear that the ability of H-NS to oligomerize is of great biological significance.
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The formation of heteromeric oligomers between related but distinct proteins is a growing theme in studies of H-NS. It is also becoming apparent that H-NS can interact with unrelated proteins.
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The finding that genes encoding proteins that are capable of interacting with H-NS can be located on mobile genetic elements has potentially important implications for the development and evolution of global regulatory circuits in bacteria.
Abstract
The effect of the bacterial heat-stable nucleoid-structuring (H-NS) protein on gene expression is overwhelmingly negative and extends throughout the genome, pointing to an almost universal role for this nucleoid-associated protein as a transcriptional repressor. Its ability to exert widespread effects on gene expression probably reflects the fact that it binds to curved DNA, which is commonly found at promoters. H-NS and related proteins can engage in both homologous and heterologous protein–protein interactions. Recent data show that the genes that encode H-NS-like proteins can be carried on mobile genetic elements. This raises the possibility that horizontal gene transfer expands the repertoire of protein–protein interactions that nucleoid-associated proteins can engage in, with potentially profound consequences for the global gene-expression profile of the cell.
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References
Ali Azam, T. & Ishihama, A. Twelve species of the nucleoid-associated protein from Escherichia coli: sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274, 33105–33113 (1999).
Ali Azam, T., Iwata, A., Nishimura, A., Ueda, S. & Ishihama, A. Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol. 181, 6361–6370 (1999).
Brunetti, R., Prosseda, G., Beghetto, E., Colonna, B. & Micheli, G. The looped domain organization of the nucleoid in histone-like protein defective Escherichia coli strains. Biochimie 83, 873–882 (2001).
Pedersen, A. G., Jensen, L. J., Brunak, S., Staerfeldt, H. H. & Ussery, D. W. A DNA structural atlas for Escherichia coli. J. Mol. Biol. 299, 907–930 (2000).
Dorman, C. J. & Deighan, P. Regulation of gene expression by histone-like proteins in bacteria. Curr. Opin. Genet. Dev. 13, 179–184 (2003).
Dersch, P., Schmidt, K. & Bremer, E. Synthesis of the Escherichia coli K-12 nucleoid-associated DNA-binding protein H-NS is subjected to growth-phase control and autoregulation. Mol. Microbiol. 8, 875–889 (1993).
Falconi, M., Brandi, A., La Teana, A., Gualerzi, C. O. & Pon, C. L. Antagonistic involvement of Fis and H-NS proteins in the transcriptional control of hns expression. Mol. Microbiol. 19, 965–975 (1996).
Free, A. & Dorman, C. J. Coupling of Escherichia coli hns mRNA levels to DNA synthesis by autoregulation: implications for growth phase control. Mol. Microbiol. 18, 101–113 (1995).
Hinton, J. C. D. et al. Expression and mutational analysis of the nucleoid-associated protein H-NS of Salmonella typhimurium. Mol. Microbiol. 6, 2327–2337 (1992).
Ueguchi, C., Kakeda, M. & Mizuno, T. Autoregulatory expression of the Escherichia coli hns gene encoding a nucleoid protein: H-NS functions as a repressor of its own transcription. Mol. Gen. Genet. 236, 171–178 (1993).
Sondén, B. & Uhlin, B. E. Coordinated and differential expression of histone-like proteins in Escherichia coli: regulation and function of the H-NS analog StpA. EMBO J. 15, 4970–4980 (1996).
Free, A. & Dorman, C. J. The Escherichia coli stpA gene is transiently expressed during growth in rich medium and is induced in minimal medium and by stress conditions. J. Bacteriol. 179, 909–918 (1997).
Deighan, P., Beloin, C. & Dorman, C. J. Three-way interactions among the Sfh, StpA and H-NS nucleoid-associated proteins of Shigella flexneri 2a strain 2457T. Mol. Microbiol. 48, 1401–1416 (2003).
Falconi, M., Higgins, N. P., Spurio, R., Pon, C. L. & Gualerzi, C. O. Expression of the gene encoding the major bacterial nucleoid protein H-NS is subject to transcriptional auto-repression. Mol. Microbiol. 10, 273–282 (1993).
Zhang, A., Rimsky, S., Reaban, M. E., Buc, H. & Belfort, M. Escherichia coli protein analogs StpA and H-NS: regulatory loops, similar and disparate effects on nucleic acid dynamics. EMBO J. 15, 1340–1349 (1996).
Dorman, C. J., Hinton, J. C. D. & Free, A. Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria. Trends Microbiol. 7, 124–128 (1999).
Schröder, O. & Wagner, R. The bacterial regulatory protein H-NS — a versatile modulator of nucleic acid structures. Biol. Chem. 383, 945–960 (2002).
Tendeng, C. & Bertin, P. H-NS in Gram-negative bacteria: a family of multifaceted proteins. Trends Microbiol. 11, 511–518 (2003).
Tupper, A. E. et al. The chromatin associated protein H-NS alters DNA topology in vitro. EMBO J. 13, 258–268 (1994).
Sonnenfield, J. M., Burns, C. M., Higgins, C. F. & Hinton, J. C. D. The nucleoid-associated protein StpA binds curved DNA, has a greater DNA-binding affinity than H-NS and is present in significant levels in hns mutants. Biochimie 83, 1–7 (2001).
Deighan, P., Free, A. & Dorman, C. J. A role for the Escherichia coli H-NS-like protein StpA in OmpF porin expression through modulation of micF RNA stability. Mol. Microbiol. 38, 126–139 (2000).
Zhang, A., Derbyshire, V., Salvo, J. L. & Belfort, M. Escherichia coli protein StpA stimulates self-splicing by promoting RNA assembly in vitro. RNA 1, 783–793 (1995).
Hommais, F. et al. Large-scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid-associated protein, H-NS. Mol. Microbiol. 40, 20–36 (2001).
Kawula, T. H. & Orndorff, P. E. Rapid site-specific DNA inversion in Escherichia coli mutants lacking the histonelike protein H-NS. J. Bacteriol. 173, 4116–4123 (1991).
O'Gara, J. P. & Dorman, C. J. Effects of local transcription and H-NS on inversion of the fim switch of Escherichia coli. Mol. Microbiol. 36, 457–466 (2000).
Starcic-Erjavec, M. et al. H-NS and Lrp serve as positive modulators of traJ expression from the Escherichia coli plasmid pRK100. Mol. Gen. Genomics 270, 94–102 (2003).
Nasser, W. & Reverchon, S. H-NS-dependent activation of pectate lyases synthesis in the phytopathogenic bacterium Erwinia chrysanthemi is mediated by the PecT repressor. Mol. Microbiol. 43, 733–748 (2002).
Bertin, P. et al. The H-NS protein is involved in the biogenesis of flagella in Escherichia coli. J. Bacteriol. 176, 5537–5540 (1994).
Ko, M. & Park, C. H-NS-dependent regulation of flagellar synthesis is mediated by a LysR-like family protein. J. Bacteriol. 182, 4670–4672 (2000).
Soutourina, O. et al. Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon. J. Bacteriol. 181, 7500–7508 (1999).
Donato, G. M. & Kawula, T. H. Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli. J. Biol. Chem. 273, 24030–24036 (1998).
Yamada, H., Muramatsu, S. & Mizuno, T. An Escherichia coli protein that preferentially binds to sharply curved DNA. J. Biochem. 108, 420–425 (1990).
Yamada, H., Yoshida, T., Tanaka, K., Sasakawa, C. & Mizuno, T. Molecular analysis of the Escherichia coli hns gene encoding a DNA binding protein which preferentially recognizes curved DNA sequences. Mol. Gen. Genet. 230, 332–336 (1991).
Bracco, L., Kotlarz, D., Kolb, A., Diekmann, S. & Buc, H. Synthetic curved DNA sequences can act as transcriptional activators in Escherichia coli. EMBO J. 8, 4289–4296 (1989).
Jauregui, R., Abreu-Goodger, C., Moreno-Hagelsieb, G., Collado-Vides, J. & Merino, E. Conservation of DNA curvature signals in regulatory regions of prokaryotic genes. Nucleic Acids Res. 31, 6770–6777 (2003).
Barbic, A., Zimmer, D. P. & Crothers, D. M. Structural origins of adenine-tract bending. Proc. Natl Acad. Sci. USA 100, 2369–2373 (2003).
La Teana, A. et al. Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS. Proc. Natl Acad. Sci. USA 88, 10907–10911 (1991).
Lease, R. A. & Belfort, M. Riboregulation by DsrA RNA: trans-actions for global economy. Mol. Microbiol. 38, 667–672 (2000).
Brescia, C. C., Mikulecky, P. J., Feig, A. L. & Sledjeski, D. D. Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure. RNA 9, 33–43 (2003).
Welch, T. J., Farewell, A., Neidhardt, F. C. & Bartlett, D. H. Stress response of Escherichia coli to elevated hydrostatic pressure. J. Bacteriol. 175, 7170–7177 (1993).
Johansson, J. & Uhlin, B. E. Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary phase survival of Escherichia coli. Proc. Natl Acad. Sci. USA 96, 10776–10781 (1999).
Reusch, R. N. et al. Posttranslational modification of E. coli histone-like protein H-NS and bovine histones by short-chain poly-(R)-3-hydroxybutyrate (cPHB). FEBS Lett. 527, 319–322 (2002). Tackles the neglected topic of small-molecule interactions with H-NS.
Schneider, D. A., Ross, W. & Gourse, R. L. Control of rRNA expression in Escherichia coli. Curr. Opin. Microbiol. 6, 151–156 (2003).
Dame, R. T., Wyman, C., Wurm, R., Wagner, R. & Goosen, N. Structural basis for H-NS mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1. J. Biol. Chem. 277, 2146–2150 (2002). Uses scanning-force microscopy to analyse the H-NS-mediated DNA bridging that prevents the elongation phase of rrnB transcription.
Beloin, C. & Dorman, C. J. An extended role for the nucleoid structuring protein H-NS in the virulence gene regulatory cascade of Shigella flexneri. Mol. Microbiol. 47, 825–838 (2003).
Caramel, A. & Schnetz, K. Lac and lambda repressors relieve silencing of the Escherichia coli bgl promoter. Activation by alteration of a repressing nucleoprotein complex. J. Mol. Biol. 284, 875–883 (1998).
Falconi, M., Prosseda, G., Giangrossi, M., Beghetto, E. & Colonna, B. Involvement of Fis in the H-NS-mediated regulation of virF gene of Shigella and enteroinvasive Escherichia coli. Mol. Microbiol. 42, 439–452 (2001). Provides a molecular explanation of the subtleties of Fis–H-NS antagonism at the virF promoter that may have implications for other genes that are subject to conflicting regulatory influences.
Haack, K. R., Robinson, C. L., Miller, K. J., Fowlkes, J. W. & Mellies, J. L. Interaction of Ler at the LEE5 (tir) operon of enteropathogenic Escherichia coli. Infect. Immun. 71, 384–392 (2003). Describes a model for Ler–H-NS antagonism at promoters within the LEE pathogenicity island. Should be read in conjunction with reference 105.
Jordi, B. J. A. M. et al. The positive regulator CfaD overcomes the repression mediated by the histone-like protein H-NS (H1) in the CFA/I fimbrial operon of Escherichia coli. EMBO J. 11, 2627–2632 (1992).
Tobe, T., Yoshikawa, M., Mizuno, T. & Sasakawa, C. Transcriptional control of the invasion regulatory gene virB of Shigella flexneri: activation by VirF and repression by H-NS. J. Bacteriol. 175, 6142–6149 (1993).
Westermark, M., Oscarsson, J., Mizunoe, Y., Urbonaviciene, J. & Uhlin, B. E. Silencing and activation of ClyA cytotoxin expression in Escherichia coli. J. Bacteriol. 182, 6347–6357 (2000).
Yu, R. R. & DiRita, V. Regulation of gene expression in Vibrio cholerae by ToxT involves both antirepression and RNA polymerase stimulation. Mol. Microbiol. 43, 119–134 (2002).
Schnetz, K. & Wang, J. C. Silencing of the Escherichia coli bgl promoter: effects of template supercoiling and cell extracts on promoter activity in vitro. Nucleic Acids Res. 24, 2422–2428 (1996).
Mukerji, M. & Mahadevan, S. Characterization of the negative elements involved in silencing the bgl operon of Escherichia coli: possible roles for DNA gyrase, H-NS, and CRP–cAMP in regulation. Mol. Microbiol. 24, 617–627 (1997).
Amit, R., Oppenheim, A. B. & Stavans, J. Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor. Biophys. J. 84, 2467–2473 (2003). Excellent single-molecule study that examines the formation of H-NS polymers on DNA.
Badaut, C. et al. The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA. J. Biol. Chem. 277, 41657–41666 (2002).
Barth, M., Marschall, C., Muffler, A., Fischer, D. & Hengge-Aronis, R. Role of the histone-like protein H-NS in growth phase-dependent and osmotic regulation of σs and many σs-dependent genes in Escherichia coli. J. Bacteriol. 177, 3455–3464 (1995).
Fletcher, S. A. & Csonka, L. N. Fine-structure deletion analysis of the transcriptional silencer of the proU operon of Salmonella typhimurium. J. Bacteriol. 177, 4508–4513 (1995).
Nieto, J. M. et al. Expression of the haemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS. Mol. Gen. Genet. 263, 349–358 (2000).
Nieto, J. M. et al. Evidence for direct protein–protein interaction between members of the Enterobacterial Hha/YmoA and H-NS families of proteins. J. Bacteriol. 184, 629–635 (2002). Shows that Hha shows homology throughout its length to the oligomerization domain of H-NS.
Porter, M. E. & Dorman, C. J. A role for H-NS in the thermo-osmotic regulation of virulence-gene expression in Shigella flexneri. J. Bacteriol. 176, 4187–4191 (1994).
Rajkumari, K., Kusano, S., Ishihama, A., Mizuno, T. & Gowrishankar, J. Effects of H-NS and potassium glutamate on σS- and σ70-directed transcription in vitro from osmotically regulated P1 and P2 promoters of proU in Escherichia coli. J. Bacteriol. 178, 4176–4181 (1996).
Gowrishankar, J. & Manna, D. How is osmotic regulation of transcription of the Escherichia coli proU operon achieved? A review and a model. Genetica 97, 363–378.
Falconi, M., Colonna, B., Prosseda, G., Micheli, G. & Gualerzi, C. O. Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS. EMBO J. 17, 7033–7043 (1998).
Rohde, J. R., Luan, X. S., Rohde, H., Fox, J. M. & Minnich, S. A. The Yersinia enterocolitica pYV virulence plasmid contains multiple intrinsic DNA bends which melt at 37 °C. J. Bacteriol. 181, 4198–4204 (1999).
Ussery, D. W., Higgins, C. F. & Bolshoy, A. Environmental influences on DNA curvature. J. Biomol. Struct. Dyn. 16, 811–823 (1999).
Sinden, R. R., Pearson, C. E., Potaman, V. N. & Ussery, D. W. DNA: structure and function. Adv. Gen. Biol. 5A, 1–141 (1998).
Ceschini, S. et al. Multimeric self-assembly equilibria involving the histone-like protein H-NS. A thermodynamic study. J. Biol. Chem. 275, 729–734 (2000).
Bloch, V. et al. The H-NS dimerization domain defines a new fold contributing to DNA recognition. Nature Struct. Biol. 10, 212–218 (2003). Defines the core dimerization motif of E. coli H-NS using NMR analysis and suggests a role for the linker region in protein–protein interactions.
Esposito, D. et al. H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein. J. Mol. Biol. 324, 841–850 (2002). Presents evidence for a head-to-tail mechanism for the assembly of H-NS polymers based on interactions between the oligomerization domains of dimers.
Cusick, M. E. & Belfort, M. E. Domain structure and RNA annealing activity of the Escherichia coli regulatory protein StpA. Mol. Microbiol. 28, 847–857 (1998).
Ueguchi, C., Seto, C., Suzuki, T. & Mizuno, T. Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS. J. Mol. Biol. 274, 145–151 (1997).
Ueguchi, C., Suzuki, T., Yoshida, T., Tanaka, K. & Mizuno, T. Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS. J. Mol. Biol. 263, 149–162 (1996).
Shindo, H. et al. Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. FEBS Lett. 360, 125–131 (1995).
Shindo, H. et al. Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy. FEBS Lett. 455, 63–69 (1999).
Smyth, C. P. et al. Oligomerization of the chromatin-structuring protein HNS. Mol. Microbiol. 36, 962–972 (2000).
Tippner, D. & Wagner, R. Fluorescence analysis of the Escherichia coli transcription regulator H-NS reveals two distinguishable complexes dependent on binding to specific or non-specific DNA sites. J. Biol. Chem. 270, 22243–22247 (1995).
Spurio, R., Falconi, M., Brandi, A., Pon, C. L. & Gualerzi, C. O. The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J. 16, 1795–1805 (1995).
Dame, R. T., Wyman, C. & Goosen, N. H-NS mediated compaction of DNA visualized by atomic force microscopy. Nucleic Acids Res. 28, 3504–3510 (2000).
Spurio, R. et al. Lethal overproduction of the Escherichia coli nucleoid protein H-NS: ultramicroscopic and molecular autopsy. Mol. Gen. Genet. 231, 201–211 (1992).
Rimsky, S., Zuber, F., Buckle, M. & Buc, H. A molecular mechanism for the repression of transcription by the H-NS protein. Mol. Microbiol. 42, 1311–1323 (2001).
Dame, R. T. & Goosen, N. HU: promoting or counteracting DNA compaction? FEBS Lett. 529, 151–156 (2002).
Free, A., Williams, R. M. & Dorman, C. J. The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli. J. Bacteriol. 180, 994–997 (1998).
Free, A., Porter, M. E., Deighan, P. & Dorman, C. J. Requirement for the molecular adapter function of StpA at the Escherichia coli bgl promoter depends upon the level of truncated H-NS protein. Mol. Microbiol. 42, 903–918 (2001).
Johansson, J., Eriksson, S., Sondén, B., Wai, S. N. & Uhlin, B. E. Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli. J. Bacteriol. 183, 2343–2347 (2001).
Williams, R. M., Rimsky, S. & Buc, H. Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins using dominant negative derivatives. J. Bacteriol. 178, 4335–4343 (1996).
Claret, L. & Rouvière-Yaniv, J. Variation in HU composition during growth of Escherichia coli: the heterodimer is required for long term survival. J. Mol. Biol. 273, 93–104 (1997).
Claret, L. & Rouvière-Yaniv, J. Regulation of HU α and HU β by CRP and FIS in Escherichia coli. J. Mol. Biol. 263, 126–139 (1996).
Tanaka, H. et al. Role of HU proteins in forming and constraining supercoils of chromosomal DNA in Escherichia coli. Mol. Gen. Genet. 248, 518–526 (1995).
Oberto, J. & Rouvière-Yaniv, J. Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium. J. Bacteriol. 178, 293–297 (1996).
Cases, I. & de Lorenzo, V. The genomes of Pseudomonas encode a third HU protein. Microbiol. 148, 1243–1245 (2002).
Fleischmann, R. D. et al. Whole-genome random sequencing of Haemophilus influenzae Rd. Science 269, 496–512 (1995).
Kajitani, M. & Ishihama, A. Identification and sequence determination of the host factor gene for bacteriophage QB . Nucleic Acids Res. 19, 1063–1066 (1991).
Muffler, A., Fischer, D., Altuvia, S., Storz, G. & Hengge-Aronis, R. The RNA binding protein HF-1, known as a host factor for phage QB RNA replication, is essential for rpoS translation in Escherichia coli. Genes Dev. 10, 1143–1151 (1996).
Nogueira, T. & Springer, M. Post-transcriptional control by global regulators of gene expression in bacteria. Curr. Opin. Microbiol. 3, 154–158 (2000).
Nieto, J. M. et al. The hha gene modulates haemolysin expression in Escherichia coli. Mol. Microbiol. 5, 1285–1293 (1991).
Robertson, C. A. & Nash, H. A. Bending of the bacteriophage λ attachment site by Escherichia coli integration host factor. J. Biol. Chem. 263, 3554–3557 (1988).
Ball, C. A. & Johnson, R. C. Multiple effects of Fis on integration and the control of lysogeny in phage λ. J. Bacteriol. 173, 4032–4038 (1991).
Liu, Q. & Richardson, C. C. Gene 5.5 protein of bacteriophage T7 inhibits the nucleoid protein H-NS of Escherichia coli. Proc. Natl Acad. Sci. USA 90, 1761–1765 (1993).
Buchrieser, C. et al. The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri. Mol. Microbiol. 38, 760–771 (2000).
Wilson, R. L. et al. Fis, a DNA nucleoid-associated protein, is involved in Salmonella typhimurium SPI-1 invasion gene expression. Mol. Microbiol. 39, 79–88 (2001).
Schechter, L. M., Jain, S., Akbar, S. & Lee, C. A. The small nucleoid-binding proteins H-NS, HU, and Fis affect hilA expression in Salmonella enterica serovar Typhimurium. Infect. Immun. 71, 5432–5435 (2003).
Nye, M. B. & Taylor, R. K. Vibrio cholerae H-NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H-NS family members. Mol. Microbiol. 50, 427–444 (2003). Discusses evidence that the H-NS protein of the pathogen Vibrio cholerae has an additional oligomerization motif in the extreme amino terminus of the protein.
Cerdan, R. et al. Crystal structure of the N-terminal dimerization domain of VicH, the H-NS-like protein of Vibrio cholerae. J. Mol. Biol. 334, 179–185 (2003). Shows that the amino-terminal domain of the Vibrio cholerae H-NS protein folds in a similar way to the Escherichia coli protein.
Bustamante, V. H., Santana, F. J., Calva, E. & Puente, J. L. Transcriptional regulation of type III secretion genes in enteropathogenic Escherichia coli: Ler antagonizes H-NS-dependent repression. Mol. Microbiol. 39, 664–678 (2001). Describes the antagonism of H-NS-mediated transcriptional repression by Ler, a protein that shares the DNA-binding domain of H-NS but not its oligomerization region. See also reference 48.
Beloin, C., Deighan, P., Doyle, M. & Dorman, C. J. Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein. Mol. Gen. Genomics 270, 66–77 (2003).
Prosseda, G. et al. The virF promoter in Shigella: more than just a curved DNA stretch. Mol. Microbiol. 51, 523–537 (2004).
Afflerbach, H., Schröder, O. & Wagner, R. Conformational changes of the upstream DNA mediated by H-NS and Fis regulate E. coli rrnB promoter activity. J. Mol. Biol. 286, 339–353 (1999).
Afflerbach, H., Schröder, O. & Wagner, R. Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo. Mol. Microbiol. 28, 641–653 (1998). Provides a vivid account of the dynamic interplay between DNA topology, nucleoid-associated proteins and temperature in promoter activation.
Rimsky, S. Structure of the histone-like protein H-NS and its role in regulation and genome superstructure. Curr. Opin. Microbiol. 7, 1–6 (2004). Provides a useful summary of the most recent structural data available for H-NS.
Acknowledgements
I thank M. Mangan, C. Conway and N. Ní Bhriain for insightful comments on the manuscript. Due to space constraints, it has not been possible to cite every relevant paper and I apologize to colleagues whose work has not been included in the references. Work on bacterial nucleoid-associated proteins in the author's laboratory is supported by Science Foundation Ireland, the Health Research Board and the Wellcome Trust.
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Glossary
- NUCLEOID
-
In bacteria, the nucleoid is defined as the region that contains the DNA genome and its associated proteins.
- PARALOGUES
-
Sequences, or genes, that have originated from a common ancestral sequence, or gene, by a duplication event.
- RNA CHAPERONES
-
Ubiquitous nucleic-acid-binding proteins that interact with RNA and can promote activities such as RNA–RNA annealing, and strand transfer and exchange.
- ANTISENSE RNA
-
A naturally occurring short, untranslated RNA transcript that often functions as a repressor of plasmid replication.
- POLY-(R)-3-HYDROXYBUTYRATE
-
A lipid homopolymer that is found in association with several membrane and cytoplasmic proteins in E. coli and is a highly efficient solute for many hydrophobic molecules.
- PERSISTENCE LENGTH
-
The average distance over which DNA adopts a straight-line trajectory in three-dimensional space. At distances greater than the persistence length, the DNA adopts a random-coil configuration.
- LON-MEDIATED PROTEOLYSIS
-
Lon is an ATP-dependent protease that is responsible for a large proportion of proteolysis in E. coli.
- INCOMPATIBILITY GROUP
-
All plasmids are grouped into incompatibility groups, that is, groups of plasmids that share similar features and are less stable in the presence of a plasmid from the same group. More than 30 incompatibility groups have been identified.
- EPISOME
-
An independent DNA element, in this case a plasmid, that can replicate extrachromosomally or that can be maintained by integrating into the genome of the host.
- α-HAEMOLYSIN TOXIN
-
A bacterial protein toxin that lyses red blood cells.
- PATHOGENICITY ISLAND
-
A contiguous block of genes, of which at least a subset code for virulence factors.
- LOCUS OF ENTEROCYTE EFFACEMENT
-
(LEE) A chromosomal pathogenicity island in enteropathogenic E. coli that includes the genes responsible for the formation of attachment and effacing (A/E) lesions.
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Dorman, C. H-NS: a universal regulator for a dynamic genome. Nat Rev Microbiol 2, 391–400 (2004). https://doi.org/10.1038/nrmicro883
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DOI: https://doi.org/10.1038/nrmicro883
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