Letteratura scientifica selezionata sul tema "Spirosomes"
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Articoli di riviste sul tema "Spirosomes"
Azmi, Liyana, Eilis C. Bragginton, Ian T. Cadby, Olwyn Byron, Andrew J. Roe, Andrew L. Lovering e Mads Gabrielsen. "High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE". Acta Crystallographica Section F Structural Biology Communications 76, n. 9 (19 agosto 2020): 414–21. http://dx.doi.org/10.1107/s2053230x20010237.
Testo completoCho, Saehyun, Gijeong Kim, Ji-Joon Song e Carol Cho. "Cryo-EM structure of Vibrio cholerae aldehyde-alcohol dehydrogenase spirosomes". Biochemical and Biophysical Research Communications 536 (gennaio 2021): 38–44. http://dx.doi.org/10.1016/j.bbrc.2020.12.040.
Testo completoNomura, Shuichi, Kuniyoshi Masuda e Tomio Kawata. "Comparative Characterization of Spirosomes Isolated fromLactobacillus brevis, Lactobacillus fermentum, andLactobacillus buchneri". Microbiology and Immunology 33, n. 1 (gennaio 1989): 23–34. http://dx.doi.org/10.1111/j.1348-0421.1989.tb01494.x.
Testo completoMatayoshi, Seiken, e Hiroshi Oda. "Detection of Fine Spiral Structures (Spirosomes) by Weak Sonication in Some Bacterial Strains". Microbiology and Immunology 29, n. 1 (gennaio 1985): 13–20. http://dx.doi.org/10.1111/j.1348-0421.1985.tb00798.x.
Testo completoLaurenceau, Raphaël, Petya V. Krasteva, Amy Diallo, Sahra Ouarti, Magalie Duchateau, Christian Malosse, Julia Chamot-Rooke e Rémi Fronzes. "Conserved Streptococcus pneumoniae Spirosomes Suggest a Single Type of Transformation Pilus in Competence". PLOS Pathogens 11, n. 4 (15 aprile 2015): e1004835. http://dx.doi.org/10.1371/journal.ppat.1004835.
Testo completoMatayoshi, S., H. Oda e G. Sarwar. "Relationship between the Production of Spirosomes and Anaerobic Glycolysis Activity in Escherichia coli B". Microbiology 135, n. 3 (1 marzo 1989): 525–29. http://dx.doi.org/10.1099/00221287-135-3-525.
Testo completoExtance, Jonathan, Susan J. Crennell, Kirstin Eley, Roger Cripps, David W. Hough e Michael J. Danson. "Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation inGeobacillus thermoglucosidasius". Acta Crystallographica Section D Biological Crystallography 69, n. 10 (20 settembre 2013): 2104–15. http://dx.doi.org/10.1107/s0907444913020349.
Testo completoAhn, Jae-Hyung, Hang-Yeon Weon, Soo-Jin Kim, Seung-Beom Hong, Soon-Ja Seok e Soon-Wo Kwon. "Spirosoma oryzae sp. nov., isolated from rice soil and emended description of the genus Spirosoma". International Journal of Systematic and Evolutionary Microbiology 64, Pt_9 (1 settembre 2014): 3230–34. http://dx.doi.org/10.1099/ijs.0.062901-0.
Testo completoFries, Julia, Stefan Pfeiffer, Melanie Kuffner e Angela Sessitsch. "Spirosoma endophyticum sp. nov., isolated from Zn- and Cd-accumulating Salix caprea". International Journal of Systematic and Evolutionary Microbiology 63, Pt_12 (1 dicembre 2013): 4586–90. http://dx.doi.org/10.1099/ijs.0.052654-0.
Testo completoHatayama, Kouta, e Teruaki Kuno. "Spirosoma fluviale sp. nov., isolated from river water". International Journal of Systematic and Evolutionary Microbiology 65, Pt_10 (1 ottobre 2015): 3447–50. http://dx.doi.org/10.1099/ijsem.0.000433.
Testo completoTesi sul tema "Spirosomes"
Lopez-Lozano, Nina. "Caractérisation structurale de nanomachines bactériennes impliquées dans l'adaptabilité et la virulence". Electronic Thesis or Diss., Bordeaux, 2023. http://www.theses.fr/2023BORD0482.
Testo completoThis thesis is divided into two themes.The first theme focuses on the cag Type IV secretion system (cag-T4SS) of the bacterium Helicobacter pylori. This is a complex secretion machinery embedded in the bacterium's cellular envelope, enabling it to inject the CagA oncoprotein into human gastric epithelial cells. This toxin is considered a major virulence factor of H. pylori. It interacts with host proteins, disrupting cell signaling and leading to changes that can promote the development of gastrointestinal diseases, including gastric ulcers and cancers. The cag-T4SS is subdivided into three parts: (i) an inner membrane complex, composed essentially of ATPases providing the energy required for its assembly and/or its function; (ii) an outer membrane complex, or core complex, forming a channel that connects the inner and outer membranes; and (iii) an extracellular pilus, the existence of which is still controversial, and which would establish contact between the bacterium and its target, and possibly transfer substrates across the host membrane.The first project focuses on the extracellular pilus. The aim is to obtain data concerning a putative interaction between the CagI and CagL proteins, which are essential for secretion and are thought to be involved in the composition of the cag-T4SS pilus. We overexpressed recombinant versions of these proteins in Escherichia coli and co-purified them by affinity chromatography, demonstrating a direct interaction between them. The ability of DARPins and Nanobodies to bind this complex was tested. Analysis of these complexes was also undertaken by cryo-electron microscopy (cryoEM).The second project focuses on the core complex, with the aim of obtaining its structure at high resolution in order to shed light on the remaining grey areas concerning this imposing assembly. Various techniques have been used to solubilize this complex. Its purification remains to be optimized before it can be analyzed by cryoEM. Obtaining such structures could lead to a better understanding of how cag-T4SS functions, and to consider strategies to inhibit its assembly and/or function, thus depriving H. pylori of a major virulence factor.The second theme concerns bacterial spirosomes. The AdhE enzyme is highly conserved in the bacterial kingdom and in certain eukaryotic organisms. It is a bifunctional alcohol/aldehyde dehydrogenase enzyme, responsible for the conversion of acetyl-CoA to acetaldehyde and then to ethanol during anaerobic alcoholic fermentation. This enzyme is commonly found in its oligomeric form, known as spirosome. Depending on the ligands present in the medium, E. coli spirosomes can have a compact or extended conformation, the latter constituting the active form of the enzyme. Unlike E. coli spirosomes, Streptococcus pneumoniae ones are naturally stabilized in their extended conformation.The aim of this project is to understand the mechanisms behind this conformational difference. CryoEM enabled us to obtain a high-resolution structure of the S. pneumoniae spirosome and thus comparing it with the extended E. coli spirosome. Functional mutagenesis experiments with complementation enabled us to determine which residues are involved in the extension of these spirosomes. As they are involved in pathogenicity and have been shown to be essential to bacterial physiology in the absence of oxygen, in-depth study of their conformation could lead to the discovery of molecules capable of regulating their activity, which could be of major interest in the fields of biotechnology and healthcare