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20 results on '"Wehenkel, Anne Marie"'

1. Molecular mechanism of a triazole-containing inhibitor of Mycobacterium tuberculosis DNA gyrase

Author

Gedeon, Antoine, Yab, Emilie, Dinut, Aurelia, Sadowski, Elodie, Capton, Estelle, Dreneau, Aurore, Petit, Julienne, Gioia, Bruna, Piveteau, Catherine, Djaout, Kamel, Lecat, Estelle, Wehenkel, Anne Marie, Gubellini, Francesca, Mechaly, Ariel, Alzari, Pedro M., Deprez, Benoît, Baulard, Alain, Aubry, Alexandra, Willand, Nicolas, and Petrella, Stéphanie

Published
2024
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7. 3D structures of the Plasmodium vivax subtilisin-like drug target SUB1 reveal conformational changes to accommodate a substrate-derived α-ketoamide inhibitor

Author

Martinez, Mariano, primary, Batista, Fernando A., additional, Maurel, Manon, additional, Bouillon, Anthony, additional, Ortega Varga, Laura, additional, Wehenkel, Anne Marie, additional, Le Chevalier-Sontag, Lucile, additional, Blondel, Arnaud, additional, Haouz, Ahmed, additional, Hernandez, Jean-François, additional, Alzari, Pedro M., additional, and Barale, Jean-Christophe, additional

Published
2023
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12. Proteome remodeling in the Mycobacterium tuberculosis PknG knockout: Molecular evidence for the role of this kinase in cell envelope biogenesis and hypoxia response

Author

Wehenkel, Anne Marie, Lima, Analía, Leyva, Alejandro, Rivera, Bernardina, Portela, María Magdalena, Gil, Magdalena, Cascioferro, Alessandro, Lisa, María-Natalia, Wehenkel, Annemarie, Bellinzoni, Marco, Carvalho, Paulo, Batthyány, Carlos, Alvarez, María, Brosch, Roland, Alzari, Pedro, Durán, Rosario, Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP), Instituto de Investigaciones Biológicas Clemente Estable [Montevideo] (IIBCE), Universidad de la República Uruguay, Pathogénomique mycobactérienne intégrée - Integrated Mycobacterial Pathogenomics, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Instituto de Biología Molecular y Celular de Rosario [Rosario] (IBR), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Universidad Nacional de Rosario [Santa Fe], Fiocruz Paraná - Instituto Carlos Chagas / Carlos Chagas Institute [Curitiba, Brésil] (ICC), Fundação Oswaldo Cruz (FIOCRUZ), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Universidad de la República [Montevideo] (UCUR), This work was supported by grants from Agencia Nacional de Investigación e Innovación, Uruguay (ANII, FCE_3_2013_1_100358 and FCE_1_2014_1_104045) and FOCEM - Fondo para la Convergencia Estructural del Mercosur (COF 03/11). MG and BR were supported by fellowships from ANII [POS_NAC_2012_1_8824, POS_NAC_2015_1_109755, POS_FCE_2015_1_1005186]. AC and RB were supported by the Agence Nationale pour la Recherche (France)., Universidad de la República [Montevideo] (UDELAR), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), and Fundação Oswaldo Cruz / Oswaldo Cruz Foundation (FIOCRUZ)

Subjects
0301 basic medicine, Proteomics, Tuberculosis, Proteome, [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph], Quantitative proteomics, Mutant, Biophysics, Serine threonine protein kinase, PknG, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Protein Serine-Threonine Kinases, Biochemistry, Mycobacterium tuberculosis, 03 medical and health sciences, Bacterial Proteins, medicine, [CHIM.CRIS]Chemical Sciences/Cristallography, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Hrp-1, Serine/Threonine protein kinase, Hypoxia, Protein kinase A, ComputingMilieux_MISCELLANEOUS, Biological Phenomena, 030304 developmental biology, Msl3, 0303 health sciences, 030102 biochemistry & molecular biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, 030306 microbiology, Kinase, medicine.disease, biology.organism_classification, 3. Good health, Cell biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], 030104 developmental biology, Mas, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Biogenesis, Intracellular
Abstract

International audience; Mycobacterium tuberculosis, the etiological agent of tuberculosis, is among the deadliest human pathogens. One of M. tuberculosis's pathogenic hallmarks is its ability to persist in a dormant state in the host. Thus, this pathogen has developed mechanisms to withstand stressful conditions found in the human host. Particularly, the Ser/Thr-protein kinase PknG has gained relevance since it regulates nitrogen metabolism and facilitates bacterial survival inside macrophages. Nevertheless, the molecular mechanisms underlying these effects are far from being elucidated. To further investigate these issues, we performed quantitative proteomic analyses of protein extracts from M. tuberculosis H37Rv and a mutant lacking pknG. We found that in the absence of PknG the mycobacterial proteome was remodeled since 5.7% of the proteins encoded by M. tuberculosis presented significant changes in its relative abundance compared with the wild-type. The main biological processes affected by pknG deletion were cell envelope components biosynthesis and response to hypoxia. Thirteen DosR-regulated proteins were underrepresented in the pknG deletion mutant, including Hrp-1, which was 12.5-fold decreased according to Parallel Reaction Monitoring experiments. Altogether, our results allow us to postulate that PknG regulation of bacterial adaptation to stress conditions might be an important mechanism underlying its reported effect on intracellular bacterial survival. SIGNIFICANCE: PknG is a Ser/Thr kinase from Mycobacterium tuberculosis with key roles in bacterial metabolism and bacterial survival within the host. However, at present the molecular mechanisms underlying these functions remain largely unknown. In this work, we evaluate the effect of pknG deletion on M. tuberculosis proteome using different approaches. Our results clearly show that the global proteome was remodeled in the absence of PknG and shed light on new molecular mechanism underlying PknG role. Altogether, this work contributes to a better understanding of the molecular bases of the adaptation of M. tuberculosis, one of the most deadly human pathogens, to its host.

Published
2021

14. Population genomics and antimicrobial resistance inCorynebacterium diphtheriae

Author

Hennart, Melanie, primary, Panunzi, Leonardo G., additional, Rodrigues, Carla, additional, Gaday, Quentin, additional, Baines, Sarah L., additional, Barros-Pinkelnig, Marina, additional, Carmi-Leroy, Annick, additional, Dazas, Melody, additional, Wehenkel, Anne-Marie, additional, Didelot, Xavier, additional, Toubiana, Julie, additional, Badell, Edgar, additional, and Brisse, Sylvain, additional

Published
2020
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15. Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation inCorynebacterium glutamicum

Author

Sogues, Adrià, primary, Martinez, Mariano, additional, Gaday, Quentin, additional, Ben-Assaya, Mathilde, additional, Graña, Martin, additional, Voegele, Alexis, additional, VanNieuwenhze, Michael, additional, England, Patrick, additional, Haouz, Ahmed, additional, Chenal, Alexandre, additional, Trépout, Sylvain, additional, Duran, Rosario, additional, Wehenkel, Anne Marie, additional, and Alzari, Pedro, additional

Published
2019
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17. Bacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes

Author

Akendengue, Lurlène, Trépout, Sylvain, Graña, Martín, Voegele, Alexis, Janke, Carsten, Raynal, Bertrand, Chenal, Alexandre, Marco, Sergio, Wehenkel, Anne Marie, Université Paris-Sud - Paris 11 (UP11), Institut Curie [Paris], Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP), Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Biophysique Moléculaire (Plate-forme), This work was supported by the Institut Curie, the Institut Pasteur, the CNRS, INSERM, DIM MALINF and the French National Research Agency., ANR-12-PDOC-0021,HetTub,Mécanismes moléculaires et fonctions de l'hétérogenéité de la tubuline(2012), ANR-10-IDEX-0001,PSL,Paris Sciences et Lettres(2010), ANR-10-EQPX-0038,MIMETIS,Microscopie Interférométrique et Microscopie Electronique en Transmission In Situ(2010), and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

Subjects
Membrane Lipids, Bacterial Proteins, Verrucomicrobia, [SDV]Life Sciences [q-bio], Cryoelectron tomography, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, macromolecular substances, Cellular microbiology, Microtubules, Cytoskeleton, Article, Cytoskeletal proteins
Abstract

International audience; Bacterial kinesin light chain is a TPR domain-containing protein encoded by the bklc gene, which co-localizes with the bacterial tubulin (btub) genes in a conserved operon in Prosthecobacter. Btub heterodimers show high structural homology with eukaryotic tubulin and assemble into head-to-tail protofilaments. Intriguingly, Bklc is homologous to the light chain of the microtubule motor kinesin and could thus represent an additional eukaryotic-like cytoskeletal element in bacteria. Using biochemical characterization as well as cryo-electron tomography we show here that Bklc interacts specifically with Btub protofilaments, as well as lipid vesicles and could thus play a role in anchoring the Btub filaments to the membrane protrusions in Prosthecobacter where they specifically localize in vivo. This work sheds new light into possible ways in which the microtubule cytoskeleton may have evolved linking precursors of microtubules to the membrane via the kinesin moiety that in today's eukaryotic cytoskeleton links vesicle-packaged cargo to microtubules.

Published
2017

18. Cryo-EM structure and polar assembly of the PS2 S-layer of Corynebacterium glutamicum .

Author

Sogues A, Sleutel M, Petit J, Megrian D, Bayan N, Wehenkel AM, and Remaut H

Abstract

The polar-growing Corynebacteriales have a complex cell envelope architecture characterized by the presence of a specialized outer membrane composed of mycolic acids. In some Corynebacteriales, this mycomembrane is further supported by a proteinaceous surface layer or 'S-layer', whose function, structure and mode of assembly remain largely enigmatic. Here, we isolated ex vivo PS2 S-layers from the industrially important Corynebacterium glutamicum and determined its atomic structure by 3D cryoEM reconstruction. PS2 monomers consist of a six-helix bundle 'core', a three-helix bundle 'arm', and a C-terminal transmembrane (TM) helix. The PS2 core oligomerizes into hexameric units anchored in the mycomembrane by a channel-like coiled-coil of the TM helices. The PS2 arms mediate trimeric lattice contacts, crystallizing the hexameric units into an intricate semipermeable lattice. Using pulse-chase live cell imaging, we show that the PS2 lattice is incorporated at the poles, coincident with the actinobacterial elongasome. Finally, phylogenetic analysis shows a paraphyletic distribution and dispersed chromosomal location of PS2 in Corynebacteriales as a result of multiple recombination events and losses. These findings expand our understanding of S-layer biology and enable applications of membrane-supported self-assembling bioengineered materials., Competing Interests: Competing interests The authors declare no competing financial interests

Published
2024
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19. Evolutionary plasticity and functional repurposing of the essential metabolic enzyme MoeA.

Author

Megrian D, Martinez M, Alzari PM, and Wehenkel AM

Abstract

MoeA, or gephyrin in higher eukaryotes, is crucial for molybdenum cofactor biosynthesis required in redox reactions. Gephyrin is a moonlighting protein also involved in postsynaptic receptor clustering, a feature thought to be a recent evolutionary trait. We showed previously that a repurposed copy of MoeA (Glp) is involved in bacterial cell division. To investigate how MoeA acquired multifunctionality, we used phylogenetic inference and protein structure analyses to understand the diversity and evolutionary history of MoeA. Glp-expressing Bacteria have at least two copies of the gene, and our analysis suggests that Glp has lost its enzymatic role. In Archaea we identified an ancestral duplication where one of the paralogs might bind tungsten instead of molybdenum. In eukaryotes, the acquisition of the moonlighting activity of gephyrin comprised three major events: first, MoeA was obtained from Bacteria by early eukaryotes, second, MogA was fused to the N-terminus of MoeA in the ancestor of opisthokonts, and finally, it acquired the function of anchoring GlyR receptors in neurons. Our results support the functional versatility and adaptive nature of the MoeA scaffold, which has been repurposed independently both in eukaryotes and bacteria to carry out analogous functions in network organization at the cell membrane.

Published
2024
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20. Bacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes.

Author

Akendengue L, Trépout S, Graña M, Voegele A, Janke C, Raynal B, Chenal A, Marco S, and Wehenkel AM

Subjects
Bacterial Proteins chemistry, Cytoskeletal Proteins metabolism, Verrucomicrobia metabolism, Verrucomicrobia ultrastructure, Bacterial Proteins metabolism, Cytoskeleton metabolism, Membrane Lipids metabolism, Microtubules metabolism
Abstract

Bacterial kinesin light chain is a TPR domain-containing protein encoded by the bklc gene, which co-localizes with the bacterial tubulin (btub) genes in a conserved operon in Prosthecobacter. Btub heterodimers show high structural homology with eukaryotic tubulin and assemble into head-to-tail protofilaments. Intriguingly, Bklc is homologous to the light chain of the microtubule motor kinesin and could thus represent an additional eukaryotic-like cytoskeletal element in bacteria. Using biochemical characterization as well as cryo-electron tomography we show here that Bklc interacts specifically with Btub protofilaments, as well as lipid vesicles and could thus play a role in anchoring the Btub filaments to the membrane protrusions in Prosthecobacter where they specifically localize in vivo. This work sheds new light into possible ways in which the microtubule cytoskeleton may have evolved linking precursors of microtubules to the membrane via the kinesin moiety that in today's eukaryotic cytoskeleton links vesicle-packaged cargo to microtubules.

Published
2017
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