Nucleoid proteins

Hayat, M.A.; Mancarella, Denise A.

doi:10.1016/0968-4328(95)00022-4

Cited by 25 publications

(24 citation statements)

References 176 publications

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“…These processes are based on the existence of multiple regulatory networks in which genes are regulated in a coordinate manner in response to environmental factors, such as temperature, osmolarity, or pH. In E. coli, numerous genes involved in adaptation to environmental challenges or in virulence are controlled by DNA-binding proteins, such as HU, integration host factor, H-NS, and FIS (24). In V. cholerae, the etiologic agent of the human diarrheal disease cholera, little is known about the presence of such a DNA-binding protein.…”

Section: Discussionmentioning

confidence: 99%

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Isolation and Characterization of vicH , Encoding a New Pleiotropic Regulator in Vibrio cholerae

et al. 2000

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During the last decade, the hns gene and its product, the H-NS protein, have been extensively studied in Escherichia coli. H-NS-like proteins seem to be widespread in gram-negative bacteria. However, unlike in E. coli and in Salmonella enterica serovar Typhimurium, little is known about their role in the physiology of those organisms. In this report, we describe the isolation of vicH, an hns-like gene in Vibrio cholerae, the etiological agent of cholera. This gene was isolated from a V. cholerae genomic library by complementation of different phenotypes associated with an hns mutation in E. coli. It encodes a 135-amino-acid protein showing approximately 50% identity with both H-NS and StpA in E. coli. Despite a low amino acid conservation in the N-terminal part, VicH is able to cross-react with anti-H-NS antibodies and to form oligomers in vitro. The vicH gene is expressed as a single gene from two promoters in tandem and is induced by cold shock. A V. cholerae wild-type strain expressing a vicH⌬92 gene lacking its 3 end shows pleiotropic alterations with regard to mucoidy and salicin metabolism. Moreover, this strain is unable to swarm on semisolid medium. Similarly, overexpression of the vicH wild-type gene results in an alteration of swarming behavior. This suggests that VicH could be involved in the virulence process in V. cholerae, in particular by affecting flagellum biosynthesis.In prokaryotic cells, the organization and/or the function of their chromosomal DNA require the involvement of proteins, generally small, abundant, and basic (24). H-NS, one of the most abundant DNA-binding proteins in enterobacteria, was isolated about 30 years ago as a transcription factor (25). It was later shown to be involved in the organization of bacterial chromosome by affecting the level of DNA condensation (45). Numerous phenotypes have been associated with hns mutations, resulting from a modification in the expression of several plasmid and chromosomal genes. Most of them are regulated by environmental parameters, such as pH, osmolarity, and temperature (2, 30), or are known to be involved in bacterial virulence, e.g., in Shigella flexneri (33).H-NS exists essentially as a homodimer and binds preferentially to curved DNA in vitro (51). No information is available concerning its three-dimensional structure, except for the organization of its C-terminal domain, which has been resolved by nuclear magnetic resonance spectroscopy (39). This region is required in DNA binding, while the N-terminal region is implicated in protein-protein interactions (49, 52). H-NS synthesis is known to be negatively autoregulated and to be induced by cold shock (2).During the past few years, the genetics of Vibrio cholerae has been extensively studied, in particular in relation with the expression of virulence factors (15,40). In contrast, nothing is known about the existence of the so-called histone-like proteins involved in the structure and function of the chromosome in this organism. Recently, we have demonstrated that H-NS and H-NS-like p...

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Section: Discussionmentioning

confidence: 99%

“…In prokaryotic cells, the organization and/or the function of their chromosomal DNA require the involvement of proteins, generally small, abundant, and basic (24). H-NS, one of the most abundant DNA-binding proteins in enterobacteria, was isolated about 30 years ago as a transcription factor (25).…”

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confidence: 99%

Isolation and Characterization of vicH , Encoding a New Pleiotropic Regulator in Vibrio cholerae

et al. 2000

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“…istone-like proteins (Hlps) are small and basic bacterial proteins involved in maintaining DNA architecture and regulating DNA transactions (1)(2)(3). Various Hlps (HU, H-NS, IHF, Dps, Fis, etc.)…”

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confidence: 99%

HupB, a Nucleoid-Associated Protein of Mycobacterium tuberculosis, Is Modified by Serine/Threonine Protein Kinases In Vivo

et al. 2014

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e HU, a widely conserved bacterial histone-like protein, regulates many genes, including those involved in stress response and virulence. Whereas ample data are available on HU-DNA communication, the knowledge on how HU perceives a signal and transmit it to DNA remains limited. In this study, we identify HupB, the HU homolog of the human pathogen Mycobacterium tuberculosis, as a component of serine/threonine protein kinase (STPK) signaling. HupB is extracted in its native state from the exponentially growing cells of M. tuberculosis H 37 Ra and is shown to be phosphorylated on both serine and threonine residues. The STPKs capable of modifying HupB are determined in vitro and the residues modified by the STPKs are identified for both in vivo and the in vitro proteins through mass spectrometry. Of the identified phosphosites, Thr 65 and Thr 74 in the DNA-embracing ␤-strand of the N-terminal domain of HupB (N-HupB) are shown to be crucial for its interaction with DNA. In addition, Arg 55 is also identified as an important residue for N-HupB-DNA interaction. N-HupB is shown to have a diminished interaction with DNA after phosphorylation. Furthermore, hupB is shown to be maximally expressed during the stationary phase in M. tuberculosis H 37 Ra, while HupB kinases were found to be constitutively expressed (PknE and PknF) or most abundant during the exponential phase (PknB). In conclusion, HupB, a DNA-binding protein, with an ability to modulate chromatin structure is proposed to work in a growth-phase-dependent manner through its phosphorylation carried out by the mycobacterial STPKs.

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“…H-NS is a nucleoid-associated protein that is required for the organization of chromosomal DNA (3,6,15,48), and it also functions as a transcription factor (18,19). We found that there are several overlapping genes whose expression levels were increased both by EvgA overproduction and by the lack of H-NS (indicated in Table 2) (18).…”

Section: Effect Of Evga On Acid Survival the List Of Upregulated Genesmentioning

confidence: 84%

Global Analysis of Genes Regulated by EvgA of the Two-Component Regulatory System in Escherichia coli

2003

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The response regulator EvgA controls expression of multiple genes conferring antibiotic resistance in Escherichia coli (K. Nishino and A. Yamaguchi, J. Bacteriol. 184:2319-2323, 2002). To understand the whole picture of EvgA regulation, DNA macroarray analysis of the effect of EvgA overproduction was performed. EvgA activated genes related to acid resistance, osmotic adaptation, and drug resistance

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Nucleoid proteins

Cited by 25 publications

References 176 publications

Isolation and Characterization of vicH , Encoding a New Pleiotropic Regulator in Vibrio cholerae

Isolation and Characterization of vicH , Encoding a New Pleiotropic Regulator in Vibrio cholerae

HupB, a Nucleoid-Associated Protein of Mycobacterium tuberculosis, Is Modified by Serine/Threonine Protein Kinases In Vivo

Global Analysis of Genes Regulated by EvgA of the Two-Component Regulatory System in Escherichia coli

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