Relevant bibliographies by topics / Expression; Function; Histone-like protein H-NS

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Expression; Function; Histone-like protein H-NS'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Expression; Function; Histone-like protein H-NS"

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Nishino, Kunihiko, and Akihito Yamaguchi. "Role of Histone-Like Protein H-NS in Multidrug Resistance of Escherichia coli." Journal of Bacteriology 186, no. 5 (2004): 1423–29. http://dx.doi.org/10.1128/jb.186.5.1423-1429.2004.

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ABSTRACT The histone-like protein H-NS is a major component of the bacterial nucleoid and plays a crucial role in global gene regulation of enteric bacteria. It is known that the expression of a variety of genes is repressed by H-NS, and mutations in hns result in various phenotypes, but the role of H-NS in the drug resistance of Escherichia coli has not been known. Here we present data showing that H-NS contributes to multidrug resistance by regulating the expression of multidrug exporter genes. Deletion of the hns gene from the ΔacrAB mutant increased levels of resistance against antibiotics
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Jian, Huahua, Guanpeng Xu, Yingbao Gai, Jun Xu, and Xiang Xiao. "The Histone-Like Nucleoid Structuring Protein (H-NS) Is a Negative Regulator of the Lateral Flagellar System in the Deep-Sea Bacterium Shewanella piezotolerans WP3." Applied and Environmental Microbiology 82, no. 8 (2016): 2388–98. http://dx.doi.org/10.1128/aem.00297-16.

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ABSTRACTAlthough the histone-like nucleoid structuring protein (H-NS) is well known for its involvement in the adaptation of mesophilic bacteria, such asEscherichia coli, to cold environments and high-pressure stress, an understanding of the role of H-NS in the cold-adapted benthic microorganisms that live in the deep-sea ecosystem, which covers approximately 60% of the earth's surface, is still lacking. In this study, we characterized the function of H-NS inShewanella piezotoleransWP3, which was isolated from West Pacific sediment at a depth of 1,914 m. Anhnsgene deletion mutant (WP3Δhns) was
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Kim, Eun A., and David F. Blair. "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, no. 19 (2015): 3110–20. http://dx.doi.org/10.1128/jb.00309-15.

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ABSTRACTA number of investigations ofEscherichia colihave suggested that the DNA-binding protein H-NS, in addition to its well-known functions in chromosome organization and gene regulation, interacts directly with the flagellar motor to modulate its function. Here, in a study initially aimed at characterizing the H-NS/motor interaction further, we identify problems and limitations in the previous work that substantially weaken the case for a direct H-NS/motor interaction. Nullhnsmutants are immotile, largely owing to the downregulation of the flagellar master regulators FlhD and FlhC. We, and
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Paytubi, Sonia, Jesús García, and Antonio Juárez. "Bacterial Hha-like proteins facilitate incorporation of horizontally transferred DNA." Open Life Sciences 6, no. 6 (2011): 879–86. http://dx.doi.org/10.2478/s11535-011-0071-3.

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AbstractHorizontal gene transfer (HGT), non-hereditary transfer of genetic material between organisms, accounts for a significant proportion of the genetic variability in bacteria. In Gram negative bacteria, the nucleoid-associated protein H-NS silences unwanted expression of recently acquired foreign DNA. This, in turn, facilitates integration of the incoming genes into the regulatory networks of the recipient cell. Bacteria belonging to the family Enterobacteriaceae express an additional protein, the Hha protein that, by binding to H-NS, potentiates silencing of HGT DNA. We provide here an o
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Castang, Sandra, and Simon L. Dove. "Basis for the Essentiality of H-NS Family Members in Pseudomonas aeruginosa." Journal of Bacteriology 194, no. 18 (2012): 5101–9. http://dx.doi.org/10.1128/jb.00932-12.

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ABSTRACTMembers of the histone-like nucleoid-structuring (H-NS) family of proteins have been shown to play important roles in silencing gene expression and in nucleoid compaction. InPseudomonas aeruginosa, the two H-NS family members MvaT and MvaU are thought to bind the same AT-rich regions of the chromosome and function coordinately to control a common set of genes. Here we present evidence that the loss of both MvaT and MvaU cannot be tolerated because it results in the production of Pf4 phage that superinfect and kill cells or inhibit their growth. Using a ClpXP-based protein depletion sys
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Stratmann, Thomas, S. Madhusudan, and Karin Schnetz. "Regulation of the yjjQ-bglJ Operon, Encoding LuxR-Type Transcription Factors, and the Divergent yjjP Gene by H-NS and LeuO." Journal of Bacteriology 190, no. 3 (2007): 926–35. http://dx.doi.org/10.1128/jb.01447-07.

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ABSTRACT The yjjQ and bglJ genes encode LuxR-type transcription factors conserved in several enterobacterial species. YjjQ is a potential virulence factor in avian pathogenic Escherichia coli. BglJ counteracts the silencing of the bgl (β-glucoside) operon by H-NS in E. coli K-12. Here we show that yjjQ and bglJ form an operon carried by E. coli K-12, whose expression is repressed by the histone-like nucleoid structuring (H-NS) protein. The LysR-type transcription factor LeuO counteracts this repression. Furthermore, the yjjP gene, encoding a membrane protein of unknown function and located ups
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Forns, Núria, Rosa C. Baños, Carlos Balsalobre, Antonio Juárez, and Cristina Madrid. "Temperature-Dependent Conjugative Transfer of R27: Role of Chromosome- and Plasmid-Encoded Hha and H-NS Proteins." Journal of Bacteriology 187, no. 12 (2005): 3950–59. http://dx.doi.org/10.1128/jb.187.12.3950-3959.2005.

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ABSTRACT IncHI plasmids encode multiple-antibiotic resistance in Salmonella enterica serovar Typhi. These plasmids have been considered to play a relevant role in the persistence and reemergence of this microorganism. The IncHI1 plasmid R27, which can be considered the prototype of IncHI plasmids, is thermosensitive for transfer. Conjugation frequency is highest at low temperature (25 to 30°C), decreasing when temperature increases. R27 codifies an H-NS-like protein (open reading frame 164 [ORF164]) and an Hha-like protein (ORF182). The H-NS and Hha proteins participate in the thermoregulation
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Sonden, B., and B. E. Uhlin. "Coordinated and differential expression of histone-like proteins in Escherichia coli: regulation and function of the H-NS analog StpA." EMBO Journal 15, no. 18 (1996): 4970–80. http://dx.doi.org/10.1002/j.1460-2075.1996.tb00877.x.

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Wang, Yan, Yiquan Zhang, Zhe Yin, et al. "H-NS represses transcription of the flagellin gene lafA of lateral flagella in Vibrio parahaemolyticus." Canadian Journal of Microbiology 64, no. 1 (2018): 69–74. http://dx.doi.org/10.1139/cjm-2017-0315.

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Swarming motility is ultimately mediated by the proton-powered lateral flagellar (laf) system in Vibrio parahaemolyticus. Expression of laf genes is tightly regulated by a number of environmental conditions and regulatory factors. The nucleoid-associated DNA-binding protein H-NS is a small and abundant protein that is widely distributed in bacteria, and H-NS-like protein-dependent expression of laf genes has been identified in Vibrio cholerae and V. parahaemolyticus. The data presented here show that H-NS acts as a repressor of the swarming motility in V. parahaemolyticus. A single σ28-depende
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Liu, Baomo, Lili Shui, Kai Zhou, et al. "Impact of Plasmid-Encoded H-NS–like Protein on blaNDM-1-Bearing IncX3 Plasmid in Escherichia coli." Journal of Infectious Diseases 221, Supplement_2 (2020): S229—S236. http://dx.doi.org/10.1093/infdis/jiz567.

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Abstract Background This study was performed to assess the role of the histone-like nucleoid-structuring (H-NS)–like protein, carried by blaNDM-1-encoding IncX3-type plasmids, in the dissemination of IncX3 plasmids. Methods The blaNDM-1-encoding IncX3 plasmids were analyzed using southern blot, conjugation, and competition assays. Virulence was evaluated with a Galleria mellonella infection model. An hns-knockout IncX3 plasmid was also constructed to identify the functions of plasmid-borne H-NS–like protein in Escherichia coli. Results The assasys detected blaNDM-1-encoding IncX3-type plasmids
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Dissertations / Theses on the topic "Expression; Function; Histone-like protein H-NS"

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Sonnenfield, Jean Marie. "Study of the StpA protein from Salmonella typhimurium and Escherichia coli." Thesis, University of Oxford, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389027.

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Cao, Wei, та 曹威. "Structural studies of two nucleoid-associated proteins : histone-like nucleoid-structuring protein H-NS and α-hemolysin expression-modulating protein Hha". Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2014. http://hdl.handle.net/10722/208420.

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In prokaryotic cells, the nucleoid contains almost all the genetic materials as well as a number of nucleoid structuring factors. The nucleoid-associated proteins (NAPs) are known to have low molecular weight and the ability to form dimer or oligomer, and most of them can bind to DNA for regulation of gene expression. The Histone-like nucleoid structuring protein H-NS, well studied as one of the NAPs, acts as a global transcriptional repressor. It has independent functional N-terminal domain for oligomerization and C-terminal domain for DNA binding, joined by a flexible linker. H-NS contribute
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Book chapters on the topic "Expression; Function; Histone-like protein H-NS"

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Wang, Huayan, Weidong Yang, and Larry Fliegel. "Identification of an HMG-like protein involved in regulation of Na+/H+ exchanger expression." In The Cellular Basis of Cardiovascular Function in Health and Disease. Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5765-4_13.

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Conference papers on the topic "Expression; Function; Histone-like protein H-NS"

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Baker, J. B., M. P. McGrogan, C. Simonsen, R. L. Gronke, and B. W. Festoff. "STRUCTURE AND PROPERTIES OF PROTEASE NEXIN I." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644765.

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Human foreskin fibroblasts secrete several different serine protease inhibitors which differ in size and protease specificities. These proteins, called protease nexins (PNs) all form SDS-resistant complexes with their protease targets. Fibroblast surface receptors recognize the protease-PN complexes and mediate their delivery to lysosomes. PNI is a 45 kilodalton glycoprotein that rapidly inhibits several arg or lys-specific proteases including trypsin, thrombin, and urokinase (k assoc.∼ 4×l06,∼ 6×105 and ∼ 2×105, m−1s−1 respectively). Like antithrombin III, PNI binds heparin and inhibits throm
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Journal articles
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