Literatura académica sobre el tema "Nucleomodulins"
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Artículos de revistas sobre el tema "Nucleomodulins"
Hanford, Hannah E., Juanita Von Dwingelo y Yousef Abu Kwaik. "Bacterial nucleomodulins: A coevolutionary adaptation to the eukaryotic command center". PLOS Pathogens 17, n.º 1 (21 de enero de 2021): e1009184. http://dx.doi.org/10.1371/journal.ppat.1009184.
Texto completoBierne, Hélène y Renaud Pourpre. "Bacterial Factors Targeting the Nucleus: The Growing Family of Nucleomodulins". Toxins 12, n.º 4 (31 de marzo de 2020): 220. http://dx.doi.org/10.3390/toxins12040220.
Texto completoKhan, Abdul Arif y Zakir Khan. "Bacterial nucleomodulins and cancer: An unresolved enigma". Translational Oncology 14, n.º 1 (enero de 2021): 100922. http://dx.doi.org/10.1016/j.tranon.2020.100922.
Texto completoBierne, Hélène y Pascale Cossart. "When bacteria target the nucleus: the emerging family of nucleomodulins". Cellular Microbiology 14, n.º 5 (23 de febrero de 2012): 622–33. http://dx.doi.org/10.1111/j.1462-5822.2012.01758.x.
Texto completoDenzer, Lea, Horst Schroten y Christian Schwerk. "From Gene to Protein—How Bacterial Virulence Factors Manipulate Host Gene Expression During Infection". International Journal of Molecular Sciences 21, n.º 10 (25 de mayo de 2020): 3730. http://dx.doi.org/10.3390/ijms21103730.
Texto completoSheshukova, Ekaterina V., Natalia M. Ershova, Fedor A. Lipskerov y Tatiana V. Komarova. "Enhanced Synthesis of Foreign Nuclear Protein Stimulates Viral Reproduction via the Induction of γ-Thionin Expression". Plants 11, n.º 12 (7 de junio de 2022): 1530. http://dx.doi.org/10.3390/plants11121530.
Texto completoShallberg, Lindsey A. y Christopher A. Hunter. "Long live the king: Toxoplasma gondii nucleomodulin inhibits necroptotic cell death". Cell Host & Microbe 29, n.º 7 (julio de 2021): 1165–66. http://dx.doi.org/10.1016/j.chom.2021.06.010.
Texto completoKlema, Valerie J., Krishna Mohan Sepuru, Nadia Füllbrunn, Tierra R. Farris, Paige S. Dunphy, Jere W. McBride, Krishna Rajarathnam y Kyung H. Choi. "Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain". PLOS ONE 13, n.º 4 (11 de abril de 2018): e0194891. http://dx.doi.org/10.1371/journal.pone.0194891.
Texto completoRaheem, Abdul, Doukun Lu, Abdul Karim Khalid, Gang Zhao, Yingjie Fu, Yingyu Chen, Xi Chen et al. "The Identification of a Novel Nucleomodulin MbovP467 of Mycoplasmopsis bovis and Its Potential Contribution in Pathogenesis". Cells 13, n.º 7 (29 de marzo de 2024): 604. http://dx.doi.org/10.3390/cells13070604.
Texto completoZhao, Gang, Doukun Lu, Shujuan Wang, Hui Zhang, Xifang Zhu, Zhiyu Hao, Ali Dawood et al. "Novel mycoplasma nucleomodulin MbovP475 decreased cell viability by regulating expression of CRYAB and MCF2L2". Virulence 13, n.º 1 (19 de septiembre de 2022): 1590–613. http://dx.doi.org/10.1080/21505594.2022.2117762.
Texto completoTesis sobre el tema "Nucleomodulins"
Schator, Daniel. "Rôle fonctionnel d'une histone désacétylase codée par Legionella pneumophila". Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS513.pdf.
Texto completoLegionella pneumophila is an intracellular bacterium that secretes over 300 proteins in the hostcell through a specialized type 4 secretion system. One of these secreted L. pneumophila effectors, RomA, was shown to directly modify the host chromatin by methylating lysine 14 of Histone H3 (H3K14), a usually acetylated residue. This led to the question how deacetylation of this mark might happen during infection. An in-depth bioinformatics search led to the identification of a protein predicted to code for a histone deacetylase (HDAC), named LphD. During my PhD, I showed that LphD is secreted into the host cell during infection and specifically targets the host cell nucleus, where it exhibits deacetylase activity with high efficiency for H3K14. Indeed, I showed that LphD deacetylates the H3K14 residue also during infection, and that the activity of LphD directly influences the levels of H3K14 methylation in infected cells, highlighting the synergy between LphD and RomA. I also could show that LphD and RomA target an endogenous chromatin binding complex, named HBO1, that contains the histone acetyltransferase KAT7, controlling the acetylation status of H3K14. RNAseq of cells infected with either wild type bacteria or the LphD and RomA knockout assessed the influence of these bacterial effectors on the host’s transcriptional landscape, in particular on genes related to immune response. The model I propose is that the two secreted effectors, LphD and RomA, work together to hijack the host’s epigenetic machinery in order to facilitate the subversion of the host immune response and promotes the intracellular replication of L. pneumophila
Nukdee, Kanjana. "Identification et caractérisation de nucleomodulines putatives chez la bactérie Mycobacterium tuberculosis". Thesis, Toulouse 3, 2015. http://www.theses.fr/2015TOU30204/document.
Texto completoThe nuclear targeting of bacterial proteins that modify host cell gene expression, the so-called nucleomodulins, has emerged as a novel mechanism contributing to virulence of several intracellular pathogens. The goal of this study was to identify nucleomodulins produced by Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), and to investigate their role upon infection of the host. We first performed a screening of Mtb genome in search of genes encoding proteins with putative eukaryotic-like nuclear localization signals (NLS). We identified two genes of Mtb, Rv0229c and Rv3876, encoding proteins that are secreted in the medium by Mtb and are localized into the nucleus when expressed in epithelial cells or in human or murine macrophages. The NLSs of these two proteins were identified and found to be essential for their nuclear localization. The gene Rv0229c, a putative RNase, is present only in pathogen species of the Mtb complex and seems to have been recently acquired by horizontal gene transfer (HGT). Rv3876 appears more widely distributed in mycobacteria, and belongs to a chromosomal region encoding proteins of the type VII secretion system ESX1, essential for virulence. Ongoing studies are currently investigating the dynamics of these proteins upon infection of host cells, and their putative role in the modulation of host cell gene expression and Mtb virulence
Pourpre, Renaud. "Caractérisation de protéines nucléaires ciblées par la bactérie pathogène Listeria monocytogenes". Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS394.
Texto completoListeria monocytogenes is an optional intracellular pathogen responsible for a severe foodborne infection called listeriosis. The study of the cellular infection process of this bacterium has shed light on various mechanisms involved in host-pathogen interactions and in the functioning of the eukaryotic cell. In particular, L. monocytogenes has emerged as one of the pioneering models in the discovery of microbial targeting of chromatin and nuclear regulators. The study of a virulence factor of L. monocytogenes, LntA, allowed the identification of one of these regulators : BAHD1. By recruiting proteins involved in the formation of heterochromatin, such as HDAC1/2 and HP1, BAHD1 stimulates the formation of a compact chromatin with a repressive effect. When epithelial cells are infected with L. monocytogenes, BAHD1 suppresses the immune response stimulated by interferons, a function inhibited by LntA. Since BAHD1 is still under-researched, the first objective for my thesis was to further characterize this epigenetic regulator. In addition, preliminary data suggested that a recently discovered virulence factor of Listeria, InlP, had the potential to be, like LntA, a nucleomodulin. My second objective was to explore this hypothesis.The results of my first axis show that BAHD1 interacts with MIER1 and that this interaction is crucial for the association of BAHD1 with HDAC1/2. We also report that BAHD1 modifies chromatin by changing histone methylation and acetylation, as well as DNA methylation, at a target gene, ESR1. These results allow us to propose that BAHD1 form, with MIER1, a scaffold assembling a new chromatin remodeling complex associated with HDAC1/2 : the BAHD1 complex. We then studied the role of BAHD1 in an organ targeted by Listeria, the brain. Our results indicate that a total deficiency in BAHD1 alters the overall transcriptome of this organ in mice. Most of the overexpressed genes are involved in nervous system functions, metabolism and neurological disorders. The predominantly downregulated genes are involved in innate immunity pathways, including interferon response genes. In addition, a haplodeficiency in Bahd1 causes behavioral problems. Compared to Bahd1+/+ mice, Bahd1+/- mice suffer from increased anxiety and changes in acoustic startle reflex. These results suggest that deregulation of BAHD1, through environmental or infectious stimuli, may have neuro-pathological effects.The second axis of my thesis focused on the study of InlP interactions with host nuclear proteins, identified by a double-hybrid screen. First, we show that InlP is an atypical internalin, with leucine-rich repeats characterized by an LPX2 motif. We then identify two nuclear proteins targeted by InlP: the splicing factor and tumor suppressor RBM5 and the corepressor RERE. When InlP is produced ectopically in human cells, it is localized in the nucleus, where it alters the formation of nuclear bodies enriched in RERE. In RBM5-overexpressing cells, InlP inhibits the pro-apoptotic effect of RBM5 and stimulates the formation of dense nuclear bodies associated with RBM5. These results suggest that InlP is a nucleomodulin acting on the assembly and disassembly of target protein storage compartments involved in the synthesis and splicing of host RNAs.This work opens perspectives in the understanding of host-pathogen interactions and in a better knowledge of patho-epigenetic mechanisms, as well as in cell biology and the understanding of membraneless nuclear organelles dynamics