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Start Over Author "Byrne, Deborah" Topic myxococcus xanthus
3 results on '"Byrne, Deborah"'

1. A divergent CheW confers plasticity to nucleoid-associated chemosensory arrays.

Author

Guiseppi A, Vicente JJ, Herrou J, Byrne D, Barneoud A, Moine A, Espinosa L, Basse MJ, Molle V, Mignot T, Roche P, and Mauriello EMF

Subjects
Bacterial Proteins genetics, Bacterial Proteins metabolism, Cell Movement, Gene Expression Regulation, Bacterial, Methyl-Accepting Chemotaxis Proteins genetics, Myxococcus xanthus genetics, Operon, Phenotype, Signal Transduction, Chemotaxis, Methyl-Accepting Chemotaxis Proteins metabolism, Myxococcus xanthus physiology
Abstract

Chemosensory systems are highly organized signaling pathways that allow bacteria to adapt to environmental changes. The Frz chemosensory system from M. xanthus possesses two CheW-like proteins, FrzA (the core CheW) and FrzB. We found that FrzB does not interact with FrzE (the cognate CheA) as it lacks the amino acid region responsible for this interaction. FrzB, instead, acts upstream of FrzCD in the regulation of M. xanthus chemotaxis behaviors and activates the Frz pathway by allowing the formation and distribution of multiple chemosensory clusters on the nucleoid. These results, together, show that the lack of the CheA-interacting region in FrzB confers new functions to this small protein., Competing Interests: The authors have declared that no competing interests exist.

Published
2019
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2. The nucleoid as a scaffold for the assembly of bacterial signaling complexes.

Author

Moine, Audrey, Espinosa, Leon, Martineau, Eugenie, Yaikhomba, Mutum, Jazleena, P. J., Byrne, Deborah, Biondi, Emanuele G., Notomista, Eugenio, Brilli, Matteo, Molle, Virginie, Gayathri, Pananghat, Mignot, Tâm, and Mauriello, Emilia M. F.

Subjects
NUCLEOIDS, CHEMORECEPTORS, MYXOCOCCUS xanthus, NUCLEOTIDE sequencing, DNA-binding proteins
Abstract

The FrzCD chemoreceptor from the gliding bacterium Myxococcus xanthus forms cytoplasmic clusters that occupy a large central region of the cell body also occupied by the nucleoid. In this work, we show that FrzCD directly binds to the nucleoid with its N-terminal positively charged tail and recruits active signaling complexes at this location. The FrzCD binding to the nucleoid occur in a DNA-sequence independent manner and leads to the formation of multiple distributed clusters that explore constrained areas. This organization might be required for cooperative interactions between clustered receptors as observed in membrane-bound chemosensory arrays. [ABSTRACT FROM AUTHOR]

Published
2017
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3. The nucleoid as a scaffold for the assembly of bacterial signaling complexes

Author

Leon Espinosa, Virginie Molle, Audrey Moine, Eugenio Notomista, Emilia M. F. Mauriello, P. Gayathri, Deborah Byrne, Tâm Mignot, Emanuele G. Biondi, Matteo Brilli, P. J. Jazleena, Eugénie Martineau, Mutum Yaikhomba, Laboratoire de chimie bactérienne (LCB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Indian Institute of Science Education and Research Pune (IISER Pune), Institut de Microbiologie de la Méditerranée (IMM), Dipartimento di Biologia, University of Naples Federico II = Università degli studi di Napoli Federico II, 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), 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), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), ANR-14-CE11-0023,Bacterial sensing,Perception microbiénne pendant les comportements sociaux(2014), Università degli studi di Napoli Federico II, Universita degli Studi di Padova, Dynamique des interactions membranaires normales et pathologiques (DIMNP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1), Moine, Audrey, Espinosa, Leon, Martineau, Eugenie, Yaikhomba, Mutum, Jazleena, P. J., Byrne, Deborah, Biondi, Emanuele, Notomista, Eugenio, Brilli, Matteo, Molle, Virginie, Gayathri, Pananghat, Mignot, Tâm, Mauriello, Emilia M. F., Università degli Studi di Padova = University of Padua (Unipd), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon

Subjects
Cancer Research, Scaffold, Cytoplasm, Cell, Restriction Fragment Mapping, chemistry.chemical_compound, Cell Signaling, Electrophoretic mobility shift assay, Myxococcus xanthus, Genetics (clinical), Staining, 0303 health sciences, Chemotaxis, Chemotaxi, Myxococcus xanthu, Specimen preparation and treatment, Cell staining, Cell biology, medicine.anatomical_structure, Cell polarity, Chemical characterization, Protein Binding, Signal Transduction, Research Article, Cell Physiology, animal structures, lcsh:QH426-470, Bacterial Protein, DNA binding assay, Biology, Research and Analysis Methods, Central region, 03 medical and health sciences, Electrophoretic Techniques, Genetic, Bacterial Proteins, medicine, Binding analysis, Membrane receptor signaling, Nucleoid, Molecular Biology Techniques, Molecular Biology, Cell fusion, 030304 developmental biology, 030306 microbiology, Gene Mapping, fungi, DAPI staining, Biology and Life Sciences, Cell Biology, biology.organism_classification, Gel electrophoresis, Ecology, Evolution, Behavior and Systematic, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, lcsh:Genetics, chemistry, Nuclear staining, bacteria, DNA
Abstract

The FrzCD chemoreceptor from the gliding bacterium Myxococcus xanthus forms cytoplasmic clusters that occupy a large central region of the cell body also occupied by the nucleoid. In this work, we show that FrzCD directly binds to the nucleoid with its N-terminal positively charged tail and recruits active signaling complexes at this location. The FrzCD binding to the nucleoid occur in a DNA-sequence independent manner and leads to the formation of multiple distributed clusters that explore constrained areas. This organization might be required for cooperative interactions between clustered receptors as observed in membrane-bound chemosensory arrays., Author summary In this work, we show that the cytoplasmic chemoreceptor of the Frz chemosensory system, FrzCD, does not bind the cytoplasmic membrane like most MCPs but bind the bacterial nucleoid directly, thus forming distributed protein clusters also containing the FrzE kinase. In vitro and in vivo experiments show that DNA-binding is not sequence-specific and is mediated by a basic aminoacid sequence of the FrzCD N-terminal domain. The deletion of this motif abolishes FrzCD DNA-binding and cooperativity in the response to signals. This work shows the importance of the nucleoid in the organization and functioning of cytoplasmic signaling systems in bacteria.

Published
2017

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