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Your search keyword '"Sara B. Hernández"' showing total 2 results
Start Over Author "Sara B. Hernández" Publisher elsevier bv
2 results on '"Sara B. Hernández"'

1. New approaches and techniques for bacterial cell wall analysis

Author

Felipe Cava and Sara B. Hernández

Subjects
Microbiology (medical), 0303 health sciences, Bacteria, 030306 microbiology, Peptidoglycan, Biology, Microbiology, Data science, Bacterial cell structure, Anti-Bacterial Agents, 03 medical and health sciences, Infectious Diseases, Bacterial Proteins, Cell Wall, 030304 developmental biology
Abstract

Peptidoglycan (PG) has remained for decades in the spotlight of the never-ending battle against pathogenic bacteria as this essential bacterial structure is one of the most successful targets for antibiotics. Most of our current understanding about the composition, architecture, and dynamics of the PG relies on techniques which have experienced great technological and methodological improvements in the past years. Here we summarize recent advances in these methods with the intention to furnish a valuable resource for both PG experts and newcomers.

Published
2021
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2. The UbiK protein is an accessory factor necessary for bacterial ubiquinone (UQ) biosynthesis and forms a complex with the UQ biogenesis factor UbiJ

Author

Christophe Velours, Mahmoud Hajj Chehade, Bruno Faivre, Bérengère Rascalou, Djemel Hamdane, Caroline Mellot-Draznieks, Ludovic Pelosi, Sara B. Hernández, Murielle Lombard, Laurent Aussel, Frédéric Barras, Cameron David Fyfe, Fabien Pierrel, Josep Casadesús, Marc Fontecave, Laurent Loiseau, David Cornu, Laboratoire de chimie bactérienne (LCB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Chaire Chimie des processus biologiques, Laboratoire de Chimie des Processus Biologiques (LCPB), Collège de France (CdF (institution))-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Collège de France (CdF (institution))-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie Bio-organique (LCB), Service de Chimie Bio-Organique et de Marquage (SCBM), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Médicaments et Technologies pour la Santé (MTS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Génomique et Évolution des Microorganismes (TIMC-IMAG-GEM), Techniques de l'Ingénierie Médicale et de la Complexité - Informatique, Mathématiques et Applications, Grenoble - UMR 5525 (TIMC-IMAG), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-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 Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-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 Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Departamento de Genética, Universidad de Sevilla, ANR-15-CE11-0001,(An)aeroUbi,Caractérisation et importance physiologique de la biosynthèse d'ubiquinone sous différentes tensions d'oxygène(2015), Collège de France - Chaire Chimie des processus biologiques, Universidad de Sevilla / University of Sevilla, and Universidad de Sevilla. Departamento de Genética

Subjects
Models, Molecular, 0301 basic medicine, BALB 3T3 Cells, Ubiquinone, Mutant, medicine.disease_cause, Biochemistry, Fatty Acids, Monounsaturated, Mice, chemistry.chemical_compound, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, Virulence, Escherichia coli Proteins, Intracellular Signaling Peptides and Proteins, Salmonella enterica, Recombinant Proteins, 3. Good health, Salmonella Infections, Female, Recombinant Fusion Proteins, Biology, Microbiology, 03 medical and health sciences, Bacterial Proteins, Biosynthesis, Terminology as Topic, Escherichia coli, medicine, Animals, Humans, Protein Interaction Domains and Motifs, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, Gene, Macrophages, Cell Biology, Bacterial Load, Peptide Fragments, RAW 264.7 Cells, 030104 developmental biology, Enzyme, chemistry, Coenzyme Q – cytochrome c reductase, Protein Multimerization, Carrier Proteins, Gene Deletion, Spleen, Biogenesis
Abstract

Ubiquinone (UQ), also referred to as coenzyme Q, is a widespread lipophilic molecule in both prokaryotes and eukaryotes in which it primarily acts as an electron carrier. Eleven proteins are known to participate in UQ biosynthesis in Escherichia coli, and we recently demonstrated that UQ biosynthesis requires additional, nonenzymatic factors, some of which are still unknown. Here, we report on the identification of a bacterial gene, yqiC, which is required for efficient UQ biosynthesis, and which we have renamed ubiK. Using several methods, we demonstrated that the UbiK protein forms a complex with the C-terminal part of UbiJ, another UQ biogenesis factor we previously identified. We found that both proteins are likely to contribute to global UQ biosynthesis rather than to a specific biosynthetic step, because both ubiK and ubiJ mutants accumulated octaprenylphenol, an early intermediate of the UQ biosynthetic pathway. Interestingly, we found that both proteins are dispensable for UQ biosynthesis under anaerobiosis, even though they were expressed in the absence of oxygen. We also provide evidence that the UbiK-UbiJ complex interacts with palmitoleic acid, a major lipid in E. coli. Last, in Salmonella enterica, ubiK was required for proliferation in macrophages and virulence in mice. We conclude that although the role of the UbiK-UbiJ complex remains unknown, our results support the hypothesis that UbiK is an accessory factor of Ubi enzymes and facilitates UQ biosynthesis by acting as an assembly factor, a targeting factor, or both. Agence Nationale de la Recherche ANR-15-CE11-0001-02 Centre National de la Recherche Scientifique PICS07279 French State Program "Investissements d'Avenir" ANR-11-LABX-0011

Published
2017
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