Relevant bibliographies by topics / Bacterial Toxin-antitoxin

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Academic literature on the topic 'Bacterial Toxin-antitoxin'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "Bacterial Toxin-antitoxin"

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Kim, Yoonji, and Jihwan Hwang. "Bacterial Toxin-antitoxin Systems and Their Biotechnological Applications." Journal of Life Science 26, no. 2 (2016): 265–74. http://dx.doi.org/10.5352/jls.2016.26.2.265.

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Walling, Lauren R., and J. Scott Butler. "Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems." Journal of Bacteriology 198, no. 24 (2016): 3287–95. http://dx.doi.org/10.1128/jb.00529-16.

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ABSTRACT Toxin-antitoxin (TA) systems are ubiquitous in bacteria and archaea, where they play a pivotal role in the establishment and maintenance of dormancy. Under normal growth conditions, the antitoxin neutralizes the toxin. However, under conditions of stress, such as nutrient starvation or antibiotic treatment, cellular proteases degrade the antitoxin, and the toxin functions to arrest bacterial growth. We characterized the specificity determinants of the interactions between VapB antitoxins and VapC toxins from nontypeable Haemophilus influenzae (NTHi) in an effort to gain a better under
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Guglielmini, Julien, and Laurence Van Melderen. "Bacterial toxin-antitoxin systems." Mobile Genetic Elements 1, no. 4 (2011): 283–306. http://dx.doi.org/10.4161/mge.18477.

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Hassan, Fatima J., Mohammed F. Al-Marjani, and Intesar N. Khelkal. "Influence of diverse pH and temperatures on the gene expression of toxin-antitoxin systems in Klebsiella pneumoniae." Advancements in Life Sciences 11, no. 4 (2024): 815. http://dx.doi.org/10.62940/als.v11i4.2836.

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Background: The type II toxin-antitoxin system consists of tightly linked genetic units that produce a toxin and its specific antitoxin. Under typical circumstances, the antitoxin neutralizes the toxic effects caused by the toxin. However, the toxin-antitoxin systems during stress regulate bacterial growth and persistence by affecting translation or DNA replication. This study aimed to assess how variations in temperature and pH stress influence the regulation of type II toxin-antitoxin gene expression within Klebsiella pneumoniae isolates.Methods: Sixty-five Klebsiella pneumoniae isolates wer
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Bourne, Christina, Kevin Snead, and Felipe Avelino da Costa Ferreira. "Fuzzy interactions maintain cognate pairings in TA systems." Structural Dynamics 12, no. 2_Supplement (2025): A153. https://doi.org/10.1063/4.0000462.

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Type II toxin-antitoxin (TA) ParDE systems are widespread in bacteria. The non-secreted protein toxin, ParE, potently inhibits DNA gyrase unless it is neutralized via direct interaction with the ParD antitoxin protein. ParDE operons encode cognate pairs, insulating from cross-interactions between structurally homologous ParE toxins that can reside in the same bacterial cell. These nano- to picomolar interactions are extensive and a model for "fuzzy" interactions, wherein the ParD antitoxin contains an unstructured region that is induced to fold by interactions with the ParE toxin. A major open
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Piscotta, Frank J., Philip D. Jeffrey, and A. James Link. "ParST is a widespread toxin–antitoxin module that targets nucleotide metabolism." Proceedings of the National Academy of Sciences 116, no. 3 (2018): 826–34. http://dx.doi.org/10.1073/pnas.1814633116.

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Toxin–antitoxin (TA) systems interfere with essential cellular processes and are implicated in bacterial lifestyle adaptations such as persistence and the biofilm formation. Here, we present structural, biochemical, and functional data on an uncharacterized TA system, the COG5654–COG5642 pair. Bioinformatic analysis showed that this TA pair is found in 2,942 of the 16,286 distinct bacterial species in the RefSeq database. We solved a structure of the toxin bound to a fragment of the antitoxin to 1.50 Å. This structure suggested that the toxin is a mono-ADP-ribosyltransferase (mART). The toxin
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Singh, Charandeep, Soni Kaundal, Amar Deep, Rishita Rohilla, Maheshwaran Velusamy, and Krishan Gopal Thakur. "Structural insights into Polymorphic toxin–Immunity pair system of Bacillus subtilis." Structural Dynamics 12, no. 2_Supplement (2025): A174. https://doi.org/10.1063/4.0000483.

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Polymorphic toxins are weapons of bacterial warfare which are being used to restrict competitors, aid kin selection and shape bacterial communities. Polymorphic toxin systems (PTS) are well studied in gram negative bacteria however there are limited studies from gram positive bacteria. In Bacillus subtilis, several members of toxin-immunity protein pairs including YeeF-YezG, YobL-Y, obK YxiD-YxxD, have been reported. There are few studies describing structural/mechanistic details of these toxin-immunity pairs. This toxin requires typeVII secretion system. We have shown that the C-terminal doma
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Nonin-Lecomte, Sylvie, Laurence Fermon, Brice Felden, and Marie-Laure Pinel-Marie. "Bacterial Type I Toxins: Folding and Membrane Interactions." Toxins 13, no. 7 (2021): 490. http://dx.doi.org/10.3390/toxins13070490.

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Bacterial type I toxin-antitoxin systems are two-component genetic modules that encode a stable toxic protein whose ectopic overexpression can lead to growth arrest or cell death, and an unstable RNA antitoxin that inhibits toxin translation during growth. These systems are widely spread among bacterial species. Type I antitoxins are cis- or trans-encoded antisense small RNAs that interact with toxin-encoding mRNAs by pairing, thereby inhibiting toxin mRNA translation and/or inducing its degradation. Under environmental stress conditions, the up-regulation of the toxin and/or the antitoxin deg
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Manikandan, Parthasarathy, Sankaran Sandhya, Kavyashree Nadig, et al. "Identification, functional characterization, assembly and structure of ToxIN type III toxin–antitoxin complex from E. coli." Nucleic Acids Research 50, no. 3 (2022): 1687–700. http://dx.doi.org/10.1093/nar/gkab1264.

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Abstract Toxin–antitoxin (TA) systems are proposed to play crucial roles in bacterial growth under stress conditions such as phage infection. The type III TA systems consist of a protein toxin whose activity is inhibited by a noncoding RNA antitoxin. The toxin is an endoribonuclease, while the antitoxin consists of multiple repeats of RNA. The toxin assembles with the individual antitoxin repeats into a cyclic complex in which the antitoxin forms a pseudoknot structure. While structure and functions of some type III TA systems are characterized, the complex assembly process is not well underst
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Alonso, Juan C. "Toxin–Antitoxin Systems in Pathogenic Bacteria." Toxins 13, no. 2 (2021): 74. http://dx.doi.org/10.3390/toxins13020074.

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Toxin–antitoxin (TA) systems, which are ubiquitously present in plasmids, bacterial and archaeal genomes, are classified as types I to VI, according to the nature of the antitoxin and to the mode of toxin inhibition [...]
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Dissertations / Theses on the topic "Bacterial Toxin-antitoxin"

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Haque, Anamul. "Differential Expression Analysis of Type II Toxin-Antitoxin Genes of Pseudomonas aeruginosa PAO1 under Different Environmental Conditions." Thesis, Virginia Tech, 2018. http://hdl.handle.net/10919/83841.

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Bacterial persistence is considered as one of the primary reason for antibiotic tolerance besides genetically acquired antibiotic resistance. Persisters are the subpopulation of a clonal bacterial population, which can survive environmental extremes and become invulnerable to stresses due to limited metabolic activities and physiological functions. Cognate toxin and antitoxin (TA) pairs, which are transcribed simultaneously from the same or different operons within the bacterial chromosomes or plasmids, play an important role for bacterial survival during stressful growth environments. Pseudo
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Catchpole, Ryan Joseph. "Evolution Of The Unnecessary : Investigating How fMet Became Central In Bacterial Translation Initiation." Thesis, University of Canterbury. School of Biological Sciences, 2015. http://hdl.handle.net/10092/10334.

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All bacteria initiate translation using formylated methionine, yet directly after translation, the formyl-group is removed. This sequence of addition and removal appears futile, yet every sequenced bacterial genome encodes the enzymes for formylation and deformylation, suggesting this process is essential. Puzzlingly, the process is absent from both Archaea and Eukaryotes, and moreover, bacterial mutants lacking both the formylase and deformylase activities are viable, albeit with a diminished growth rate. We created an Escherichia coli strain devoid of formylase and deformylase activity. This
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Wilbaux, Myriam. "Le système toxine-antitoxine ccdO157 d'Escherichia coli: caractérisation fonctionelle et distribution." Doctoral thesis, Universite Libre de Bruxelles, 2008. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210503.

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Les systèmes toxine-antitoxine (TA) bactériens ont été découverts il y a une vingtaine d’année sur les plasmides à bas nombre de copie. Ils sont composés de deux gènes organisés en opéron, l’un codant pour une toxine stable et l’autre pour une antitoxine instable capable de neutraliser l’effet de la toxine. Les systèmes TA sont fortement représentés au sein de l’ensemble des génomes bactériens. Ils se localisent aussi bien sur des éléments génétiques mobiles (plasmides, phages, transposons,…) que dans les chromosomes, ce qui suggère que le transfert horizontal de gènes participe à leur dissémi
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Aakre, Christopher David. "Toxin-antitoxin systems in bacteria : targets, mechanisms, and specificity." Thesis, Massachusetts Institute of Technology, 2015. http://hdl.handle.net/1721.1/101824.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.<br>Title as it appears in MIT Commencement Exercises program, June, 2015: Toxin-antitoxin systems in bacteria : targets, mechanisms, and specificity. Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>Toxin-antitoxin (TA) systems are genetic modules widely present on bacterial chromosomes. These systems comprise a toxin and cognate antitoxin that are encoded together in an operon; normally, the toxin and antitoxin are synthesized and form a non-toxic complex. Under times of stress,
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Rocker, Andrea [Verfasser], and Ilme [Akademischer Betreuer] Schlichting. "Epsilon/Zeta Toxin-Antitoxin Systems in Gram-negative Bacteria / Andrea Rocker ; Betreuer: Ilme Schlichting." Heidelberg : Universitätsbibliothek Heidelberg, 2016. http://d-nb.info/1180614038/34.

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Jadhav, Pankaj Vilas. "Structural insights into assembly and regulation of HigBA toxin-antitoxin system from Escherichia coli." Thesis, 2021. https://etd.iisc.ac.in/handle/2005/5902.

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In the last few decades, bacterial Toxin-antitoxin (TA) systems have been identified to play crucial roles in bacterial survival under stressful conditions and virulence. TA systems are pair of genetic elements where one of the genes codes for a protein (toxin), which is toxic to the host cell, and the other gene code for its antidote (antitoxin), which can be an RNA or a protein. Under favourable growth conditions, the antitoxin inhibits the toxin activity; however, when the bacterial cell encounters stressful conditions such as antibiotic exposure, starvation, phage infection, etc., the toxi
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Manikandan, P. "Identification, characterization, structure, and assembly of type III toxin-antitoxin systems from Escherichia coli." Thesis, 2021. https://etd.iisc.ac.in/handle/2005/5633.

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Bacteria adopt several defense strategies to enable their survival against the environmental threats they encounter from time to time. Toxin-antitoxin (TA) systems are being understood as a key bacterial defense mechanism against invading viruses, antibiotics, and other environmental stress. TA systems consist of a pair of genes, usually under a common promoter, that code for a toxin and its cognate antitoxin . The toxin is usually a protein, that arrests cellular growth during stress, whereas the antitoxin can be a protein or a non-coding RNA, that inhibits the toxin. The TA systems are class
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Books on the topic "Bacterial Toxin-antitoxin"

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Toxin-Antitoxin Systems in Pathogenic Bacteria. MDPI, 2021. http://dx.doi.org/10.3390/books978-3-0365-0675-3.

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Toxin-Antitoxin Systems in Pathogenic Bacteria. Mdpi AG, 2021.

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Book chapters on the topic "Bacterial Toxin-antitoxin"

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Bendtsen, Kirstine L., and Ditlev E. Brodersen. "Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes." In Subcellular Biochemistry. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46503-6_14.

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Fleming, Brittany A., and Matthew A. Mulvey. "Toxin-antitoxin Systems as Regulators of Bacterial Fitness and Virulence." In Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria. John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119004813.ch39.

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Nielsen, Maria Raadkjær, and Ditlev E. Brodersen. "Structural Variations and Rearrangements in Bacterial Type II Toxin-Antitoxin Systems." In Subcellular Biochemistry. Springer International Publishing, 2024. http://dx.doi.org/10.1007/978-3-031-58843-3_11.

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Alonso, Juan C., Dolors Balsa, Izhack Cherny, et al. "Bacterial Toxin-Antitoxin Systems as Targets for the Development of Novel Antibiotics." In Enzyme-Mediated Resistance to Antibiotics. ASM Press, 2014. http://dx.doi.org/10.1128/9781555815615.ch19.

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Butt, Aaron T., and Richard W. Titball. "Functional Analysis of the Role of Toxin–Antitoxin (TA) Loci in Bacterial Persistence." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-2854-5_11.

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Yamaguchi, Yoshihiro, and Masayori Inouye. "Toxin-Antitoxin Systems in Bacteria and Archaea." In Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria. John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119004813.ch8.

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Masachis, Sara, and Fabien Darfeuille. "Type I Toxin-Antitoxin Systems: Regulating Toxin Expression via Shine-Dalgarno Sequence Sequestration and Small RNA Binding." In Regulating with RNA in Bacteria and Archaea. ASM Press, 2018. http://dx.doi.org/10.1128/9781683670247.ch11.

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Sužiedėlienė, Edita, Milda Jurėnaitė, and Julija Armalytė. "Identification and Characterization of Type II Toxin-Antitoxin Systems in the Opportunistic PathogenAcinetobacter Baumannii." In Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria. John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119004813.ch41.

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Kędzierska, Barbara, and Finbarr Hayes. "Transcriptional Control of Toxin-Antitoxin Expression: Keeping Toxins Under Wraps Until the Time is Right." In Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria. John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119004813.ch42.

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Allchin, Douglas. "Nobel Ideals and Noble Errors." In Sacred Bovines. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780190490362.003.0017.

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Christiaan Eijkman shared a 1929 Nobel Prize “for his discovery of the antineuritic vitamin.” His extensive studies on chickens and prison inmates on the island of Java in the 1890s helped establish a white rice diet as a cause of beriberi, and the rice coating as a remedy. Eijkman reported that he had traced a bacterial disease, its toxin, and its antitoxin. Beriberi, however, is a nutrient deficiency. Eijkman was wrong. Ironically, Eijkman even rejected the current explanation when it was first introduced in 1910. Although he earned a Nobel Prize for his important contribution on the role of
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