Proteins from the Prokaryotic Nucleoid: Biochemical and 1H NMR Studies on Three Bacterial Histone-Like Proteins

Lammi, M.; Paci, Maurizio; Pon, Cynthia L.; Losso, Maria Adele; Miano, Antonino; Pawlik, R. T.; Gianfranceschi, G.; Gualerzi, Claudio O.

doi:10.1007/978-1-4684-8730-5_48

Cited by 35 publications

(15 citation statements)

References 12 publications

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“…Here we have shown that H-NS binds more tightly to DNA than NS and, unlike the latter [15], prefers dsDNA to ssDNA, and DNA to RNA. Furthermore, we have found that, unlike that of NS [7], binding of H-NS to DNA does not show any indication of cooperativity and is stimulated by magnesium as well as by monovalent cations.…”

Section: Discussionmentioning

confidence: 74%

“…One of these, H-NS, is an abundant (-20000 copies/Escherichia coli cell), neutral (pI = 7.3), heat-stable protein with a molecular mass Correspondence address: K. Friedrich, Max-Planck-Institut fiir Molekulare Genetik, Abt. Wittmann, D-1000 Berlin 33, Germany of 15.4 kDa [7]. It is likely that H-NS corresponds to the 17 kDa protein B1 found by Varshavsky et al [8] in a 1:2 molar ratio with B2 (i.e.…”

Section: Introductionmentioning

confidence: 83%

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Proteins from the prokaryotic nucleoid Interaction of nucleic acids with the 15 kDa Escherichia coli histone‐like protein H‐NS

Friedrich¹,

Gualerzi²,

Lammi³

et al. 1988

FEBS Letters

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The interaction between nucleic acids and Escherichia coil H-NS, an abundant 15 kDa histone-like protein, has been studied by affinity chromatography, nitrocellulose filtration and fluorescence spectroscopy. Intrinsic fluorescence studies showed that the single Trp residue of H-NS (position 108) has a restricted mobility and is located within an hydrophobic region inaccessible to both anionic and cationic quenchers. Binding of H-NS to nucleic acids, however, results in a change of the microenvironment of the Trp residue and fluorescence quenching; from the titration curves obtained with addition of increasing amounts of poly(dA)-poly(dT) and poly(dC)-poly(dG) it can be estimated that an H-NS dimer in 1.5 x SSC binds DNA with an apparent Ka" 1.1 x 104 M -~ -bp-L H-NS binds to double-stranded DNA with a higher affinity than the more abundant histone-like protein NS(HU) and, unlike NS, prefers double-stranded to single-stranded DNA and DNA to RNA; both monovalent and divalent cations are required for optimal binding.

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Section: Discussionmentioning

confidence: 74%

Section: Introductionmentioning

confidence: 83%

Proteins from the prokaryotic nucleoid Interaction of nucleic acids with the 15 kDa Escherichia coli histone‐like protein H‐NS

Friedrich¹,

Gualerzi²,

Lammi³

et al. 1988

FEBS Letters

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“…Thus PHMB tolerance in E. coli was directly correlated with the level of H-NS expression. Because H-NS globally represses many unrelated genes (Lammi et al, 1984), the apparent sensitivity in the hns knockout strain could be caused by a deregulation of H-NS-regulated genes, but it could also be caused by a change in DNA structure. H-NS regulates by binding to at least two patches of curved DNA to create loops in which RNA polymerase is trapped (Dorman, 2004;Dorman & Deighan, 2003).…”

Section: Dna-binding Proteinsmentioning

confidence: 99%

The response of Escherichia coli to exposure to the biocide polyhexamethylene biguanide

2006

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The global response of Escherichia coli to the broad-spectrum biocide polyhexamethylene biguanide (PHMB) was investigated using transcriptional profiling. The transcriptional analyses were validated by direct determination of the PHMB-tolerance phenotypes of derivatives of E. coli MG1655 carrying either insertionally inactivated genes and/or plasmids expressing the cognate open reading frames from a heterologous promoter in the corresponding chromosomally inactivated strains. The results showed that a wide range of genes was altered in transcriptional activity and that all of the corresponding knockout strains subsequently challenged with biocide were altered in tolerance. Of particular interest was the induction of the rhs genes and the implication of enzymes involved in the repair/binding of nucleic acids in the generation of tolerance, suggesting a novel dimension in the mechanism of action of PHMB based on its interaction with nucleic acids.

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“…Further analysis revealed that H-NS is a DNA-binding protein that is able to condense DNA in vitro and in vivo, in a way that is similar to eukaryotic histones (Spassky et al, 1984;Spurio et al, 1992). This led to the name histone-like nucleoid structuring protein, H-NS (Lammi et al, 1984). However, H-NS does not have any sequence homology with histones and therefore we prefer the notation chromatin-or nucleoid-associated protein.…”

Section: Introductionmentioning

confidence: 99%

H‐NS: a modulator of environmentally regulated gene expression

Atlung

Ingmer

1997

Molecular Microbiology

453

409

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SummaryH-NS is a small chromatin-associated protein found in enterobacteria. H-NS has affinity for all types of nucleic acids but binds preferentially to intrinsically curved DNA. The major role of H-NS is to modulate the expression of a large number of genes, mostly by negatively affecting transcription. Many of the H-NS-modulated genes are regulated by environmental signals, and expression of most of these genes is positively regulated by specific transcription factors. Therefore one of the purposes of H-NS could be to repress expression of some genes under conditions characteristic of a non-intestinal environment, but allow expression of specific genes in response to certain stimuli in the intestinal environment. The hns gene is autoregulated. In vivo the H-NS to DNA ratio is fairly constant except during cold shock, when it increases threeto fourfold. In this review we propose that only the preferential binding to intrinsically curved DNA plays a role under normal growth conditions, and we discuss the different mechanisms by which H-NS might affect gene expression and how H-NS could be involved in the response to different stress situations. Finally, we summarize the evolutionary and functional relationship between H-NS and the homologous StpA.

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Proteins from the Prokaryotic Nucleoid: Biochemical and 1H NMR Studies on Three Bacterial Histone-Like Proteins

Cited by 35 publications

References 12 publications

Proteins from the prokaryotic nucleoid Interaction of nucleic acids with the 15 kDa Escherichia coli histone‐like protein H‐NS

Proteins from the prokaryotic nucleoid Interaction of nucleic acids with the 15 kDa Escherichia coli histone‐like protein H‐NS

The response of Escherichia coli to exposure to the biocide polyhexamethylene biguanide

H‐NS: a modulator of environmentally regulated gene expression

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