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6 results on '"Frédéric Galisson"'

1. Exploring molecular determinants of polysaccharide lyase family 6–1 enzyme activity

Author

Sébastien Violot, Vinesh Jugnarain, Loic Carrique, William Helbert, Nushin Aghajari, Lionel Ballut, Xavier Robert, Aurélien Thureau, Frédéric Galisson, Léa Conchou, Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur les Macromolécules Végétales (CERMAV ), and Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Models, Molecular, CAZy, Subfamily, [SDV]Life Sciences [q-bio], 010402 general chemistry, Crystallography, X-Ray, 01 natural sciences, Biochemistry, Substrate Specificity, protein-carbohydrates recognition, 03 medical and health sciences, Carbohydrate Conformation, Humans, Amino Acid Sequence, Binding site, Mode of action, 030304 developmental biology, Polysaccharide-Lyases, chemistry.chemical_classification, 0303 health sciences, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], structure of alginate lyases, Substrate (chemistry), Enzyme assay, 0104 chemical sciences, Enzyme, chemistry, surface-binding site, Docking (molecular), biology.protein
Abstract

The polysaccharide lyase family 6 (PL6) represents one of the 41 polysaccharide lyase families classified in the CAZy database with the vast majority of its members being alginate lyases grouped into three subfamilies, PL6_1–3. To decipher the mode of recognition and action of the enzymes belonging to subfamily PL6_1, we solved the crystal structures of Pedsa0632, Patl3640, Pedsa3628 and Pedsa3807, which all show different substrate specificities and mode of action (endo-/exolyase). Thorough exploration of the structures of Pedsa0632 and Patl3640 in complex with their substrates as well as docking experiments confirms that the conserved residues in subsites −1 to +3 of the catalytic site form a common platform that can accommodate various types of alginate in a very similar manner but with a series of original adaptations bringing them their specificities of action. From comparative studies with existing structures of PL6_1 alginate lyases, we observe that in the right-handed parallel β-helix fold shared by all these enzymes, the substrate-binding site harbors the same overall conserved structures and organization. Despite this apparent similarity, it appears that members of the PL6_1 subfamily specifically accommodate and catalyze the degradation of different alginates suggesting that this common platform is actually a highly adaptable and specific tool.

Published
2021

2. PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae

Author

Patrice Gouet, Sébastien Guiral, Frédéric Galisson, Pierre Simon Garcia, Laure Zucchini, Chryslène Mercy, Céline Brochier-Armanet, Christophe Grangeasse, Caroline Cluzel, Virginie Gueguen-Chaignon, Céline Freton, Bioinformatique, phylogénie et génomique évolutive (BPGE), Département PEGASE [LBBE] (PEGASE), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), and Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Microbiology (medical), Models, Molecular, Cell division, [SDV]Life Sciences [q-bio], 030106 microbiology, Immunology, Cell, Protein Serine-Threonine Kinases, Applied Microbiology and Biotechnology, Microbiology, Cell wall, 03 medical and health sciences, Protein structure, Bacterial Proteins, Cell Wall, Genetics, Extracellular, medicine, Amino Acid Sequence, Phosphorylation, Protein kinase A, Peptide sequence, ComputingMilieux_MISCELLANEOUS, Chemistry, food and beverages, Cell Biology, N-Acetylmuramoyl-L-alanine Amidase, Cell biology, Protein Structure, Tertiary, medicine.anatomical_structure, Streptococcus pneumoniae, Protein Kinases, Cell Division
Abstract

Eukaryotic-like serine/threonine kinases (eSTKs) with extracellular PASTA repeats are key membrane regulators of bacterial cell division. How PASTA repeats govern eSTK activation and function remains elusive. Using evolution- and structural-guided approaches combined with cell imaging, we disentangle the role of each PASTA repeat of the eSTK StkP from Streptococcus pneumoniae. While the three membrane-proximal PASTA repeats behave as interchangeable modules required for the activation of StkP independently of cell wall binding, they also control the septal cell wall thickness. In contrast, the fourth and membrane-distal PASTA repeat directs StkP localization at the division septum and encompasses a specific motif that is critical for final cell separation through interaction with the cell wall hydrolase LytB. We propose a model in which the extracellular four-PASTA domain of StkP plays a dual function in interconnecting the phosphorylation of StkP endogenous targets along with septal cell wall remodelling to allow cell division of the pneumococcus.

Published
2018

3. Expanding the Kinome World: A New Protein Kinase Family Widely Conserved in Bacteria

Author

Maria-Halima Laaberki, Marie-Pierre Candusso, Sébastien Guiral, Frédéric Galisson, Jihad Attieh, Sylvain D. Vallet, Lionel Ballut, Laure Zucchini, Adeline Page, Salsabil Kesraoui, Christophe Grangeasse, Nushin Aghajari, Jean-Michel Jault, Cédric Orelle, Hien-Anh Nguyen, Takla El Khoury, Juliette Martin, Anne-Emmanuelle Foucher, Laboratoire de microbiologie et génétique moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Epigenetique et Cancer, Centre National de la Recherche Scientifique (CNRS), Centre de génétique moléculaire (CGM), Department of Chemistry, Purdue University [West Lafayette], Unité Mathématique Informatique et Génome (MIG), Institut National de la Recherche Agronomique (INRA), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Bases moléculaires et structurales des systèmes infectieux (BMSSI), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Laboratoire de microbiologie et génétique moléculaires ( LMGM ), Université Paul Sabatier - Toulouse 3 ( UPS ) -Centre National de la Recherche Scientifique ( CNRS ), Pathogènes émergents et rongeurs sauvages ( USC1233/PERS ), Université de Lyon-VetAgro Sup ( VAS ), Centre National de la Recherche Scientifique ( CNRS ), Centre de génétique moléculaire ( CGM ), Unité Mathématique Informatique et Génome ( MIG ), Institut National de la Recherche Agronomique ( INRA ), Institut de Génétique et de Biologie Moléculaire et Cellulaire ( IGBMC ), Bases moléculaires et structurales des systèmes infectieux ( BMSSI ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Institut de biologie et chimie des protéines [Lyon] ( IBCP ), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Laboratoire de microbiologie et génétique moléculaires - UMR5100 (LMGM), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Paraquat, [SDV]Life Sciences [q-bio], 030106 microbiology, Mutant, Bacillus subtilis, [ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Biology, Crystallography, X-Ray, 03 medical and health sciences, [ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Structural Biology, Kinome, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Kinase activity, Phosphorylation, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Protein kinase A, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, ComputingMilieux_MISCELLANEOUS, [ SDV ] Life Sciences [q-bio], Kinase, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, biology.organism_classification, Oxidants, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Oxidative Stress, Biochemistry, Signal transduction, Protein Kinases, Protein Processing, Post-Translational, Gene Deletion
Abstract

Fine tuning of signaling pathways is essential for cells to cope with sudden environmental variations. This delicate balance is maintained in particular by protein kinases that control the activity of target proteins by reversible phosphorylation. In addition to homologous eukaryotic enzymes, bacteria have evolved some specific Ser/Thr/Tyr protein kinases without any structural resemblance to their eukaryotic counterparts. Here, we show that a previously identified family of ATPases, broadly conserved among bacteria, is in fact a new family of protein kinases with a Ser/Thr/Tyr kinase activity. A prototypic member of this family, YdiB from Bacillus subtilis , is able to autophosphorylate and to phosphorylate a surrogate substrate, the myelin basic protein. Two crystal structures of YdiB were solved (1.8 and 2.0 A) that display a unique ATP-binding fold unrelated to known protein kinases, although a conserved HxD motif is reminiscent of that found in Hanks-type protein kinases. The effect of mutations of conserved residues further highlights the unique nature of this new protein kinase family that we name ubiquitous bacterial kinase. We investigated the cellular role of YdiB and showed that a ∆ ydiB mutant was more sensitive to paraquat treatment than the wild type, with ~ 13% of cells with an aberrant morphology. In addition, YdiE, which is known to participate with both YdiC and YdiB in an essential chemical modification of some specific tRNAs, is phosphorylated in vitro by YdiB. These results expand the boundaries of the bacterial kinome and support the involvement of YdiB in protein translation and resistance to oxidative stress in B. subtilis.

Published
2017

4. Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments

Author

Frédéric Galisson, Maria Cristina De Rosa, Serena Vitale, Davide Pirolli, Patrice Gouet, Stéphane Réty, Benedetta Righino, Laboratoire Epigenetique et Cancer, Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)

Subjects
penicillin-binding protein and serine/threonine kinase associated, SAXS, StkP, eSTKs, Models, Molecular, 0301 basic medicine, Cell division, [SDV]Life Sciences [q-bio], 030106 microbiology, Molecular Conformation, Peptidoglycan, Molecular Dynamics Simulation, Protein Serine-Threonine Kinases, Biology, Structure-Activity Relationship, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Structural Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Protein Interaction Domains and Motifs, Amino Acid Sequence, eukaryotic-like serine/threonine protein kinases, modeling, molecular dynamics, muropeptide docking, Protein kinase A, Molecular Biology, ComputingMilieux_MISCELLANEOUS, ASTA domain, PASTA, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], General Medicine, Recombinant Proteins, PASTA domain, Cell biology, Molecular Docking Simulation, Transmembrane domain, Streptococcus pneumoniae, 030104 developmental biology, Protein kinase domain, chemistry, Biochemistry, Docking (molecular), Intracellular, Protein Binding
Abstract

The unique eukaryotic-like Ser/Thr protein kinases of Streptococcus pneumoniae, StkP, plays a primary role in the cell division process. It is composed of an intracellular kinase domain, a transmembrane helix and four extracellular PASTA subunits. PASTA domains were shown to interact with cell wall fragments but the key questions related to the molecular mechanism governing ligand recognition remain unclear. To address this issue, the full-length structural model of StkP was generated by combining small-angle X-ray scattering data with the results of computer simulations. Docking and molecular dynamics studies on the generated three-dimensional model structure reveal the possibility of peptidoglycan fragment binding at the hinge regions between PASTA subunits with a preference for a bent hinge between PASTA3 and PASTA4.

Published
2017
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5. Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae

Author

Anne-Marie Di Guilmi, Frédéric Galisson, Christophe Grangeasse, Céline Freton, Sébastien Guiral, Aurore Fleurie, Isabelle Zanella-Cléon, and Caroline Cluzel

Subjects
0303 health sciences, Cell division, 030306 microbiology, Kinase, Biology, Microbiology, Phenotype, Serine, 03 medical and health sciences, chemistry.chemical_compound, chemistry, Biochemistry, Cytoplasm, Phosphorylation, Peptidoglycan, Kinase activity, Molecular Biology, 030304 developmental biology
Abstract

Eukaryotic-like serine/threonine-kinases are involved in the regulation of a variety of physiological processes in bacteria. In Streptococcus pneumoniae, deletion of the single serine/threonine-kinase gene stkP results in an aberrant cell morphology suggesting that StkP participates in pneumococcus cell division. To understand the function of StkP, we have engineered various pneumococcus strains expressing truncated or kinase-dead forms of StkP. We show that StkP kinase activity, but also its extracellular and cytoplasmic domains per se, are required for pneumococcus cell division. Indeed, we observe that mutant cells show round or elongated shapes with non-functional septa and a chain phenotype, delocalized sites of peptidoglycan synthesis and diffused membrane StkP localization. To gain understanding of the underlying StkP-mediated regulatory mechanism, we show that StkP specifically phosphorylates in vivo the cell division protein DivIVA on threonine 201. Pneumococcus cells expressing non-phosphorylatable DivIVA-T201A possess an elongated shape with a polar bulge and aberrant spatial organization of nascent peptidoglycan. This brings the first evidence of the importance of StkP in relationship to the phosphorylation of one of its substrates in cell division. It is concluded that StkP is a multifunctional protein that plays crucial functions in pneumococcus cell shape and division.

Published
2012

6. HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2

Author

Frédéric Galisson, Nadine Assrir, Odile Filhol, Marc Lipinski, Laboratoire de génétique et biologie cellulaire (LGBC), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ), Département Réponse et Dynamique Cellulaires, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Epigenetique et Cancer, Centre National de la Recherche Scientifique (CNRS), Interactions moléculaires et cancer (IMC (UMR 8126)), Signalisation, noyaux et innovations en cancérologie (UMR8126), Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS), Dambo, Marie-Annie, Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL), and Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-École Pratique des Hautes Études (EPHE)

Subjects
Clinical Biochemistry, MESH: Rabbits, Cell Cycle Proteins, MESH: Casein Kinase II, MESH: Amino Acid Sequence, Mitogen-activated protein kinase kinase, Biochemistry, 0302 clinical medicine, Protein Interaction Mapping, MESH: Animals, Phosphorylation, Nuclear protein, Casein Kinase II, 0303 health sciences, Chemistry, Nuclear Proteins, Chromatin, Cell biology, 030220 oncology & carcinogenesis, Rabbits, Casein kinase 2, DNA, Complementary, Molecular Sequence Data, MESH: Carrier Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, MESH: Two-Hybrid System Techniques, 03 medical and health sciences, Two-Hybrid System Techniques, Animals, Humans, Amino Acid Sequence, Molecular Biology, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, 030304 developmental biology, MAPK14, Serine/threonine-specific protein kinase, MESH: K562 Cells, MESH: Humans, MESH: Molecular Sequence Data, MESH: Phosphorylation, fungi, MESH: Protein Interaction Mapping, MESH: DNA, Complementary, MESH: Hela Cells, Phosphoprotein, Cyclin-dependent kinase 9, Carrier Proteins, K562 Cells, MESH: Nuclear Proteins, HeLa Cells
Abstract

The HIRIP3 protein had been identified from its interaction with the HIRA histone chaperone. Experiments using anti-peptide antisera indicated that this 556-aa protein is nuclear throughout the cell cycle and excluded from condensed chromatin during mitosis. Based on its electrophoretic migration and sensitivity to phosphatase treatment, endogenous HIRIP3 was found to be heavily phosphorylated. HIRIP3 can be phosphorylated in vitro by a recombinant form of the serine-threonine kinase CK2. Moreover, HIRIP3 protein was found to co-purify with a CK2 activity. Together, these data prompt us to propose HIRIP3 as a new member of the growing list of CK2 substrates with a possible role in chromatin metabolism.

Published
2007

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