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  1. Article ; Online: The transpeptidase PBP2 governs initial localization and activity of the major cell-wall synthesis machinery in E. coli

    Gizem Özbaykal / Eva Wollrab / Francois Simon / Antoine Vigouroux / Baptiste Cordier / Andrey Aristov / Thibault Chaze / Mariette Matondo / Sven van Teeffelen

    eLife, Vol

    2020  Volume 9

    Abstract: Bacterial shape is physically determined by the peptidoglycan cell wall. The cell-wall-synthesis machinery responsible for rod shape in Escherichia coli is the processive 'Rod complex'. Previously, cytoplasmic MreB filaments were thought to govern ... ...

    Abstract Bacterial shape is physically determined by the peptidoglycan cell wall. The cell-wall-synthesis machinery responsible for rod shape in Escherichia coli is the processive 'Rod complex'. Previously, cytoplasmic MreB filaments were thought to govern formation and localization of Rod complexes based on local cell-envelope curvature. Using single-particle tracking of the transpeptidase and Rod-complex component PBP2, we found that PBP2 binds to a substrate different from MreB. Depletion and localization experiments of other putative Rod-complex components provide evidence that none of those provide the sole rate-limiting substrate for PBP2 binding. Consistently, we found only weak correlations between MreB and envelope curvature in the cylindrical part of cells. Residual correlations do not require curvature-based Rod-complex initiation but can be attributed to persistent rotational motion. We therefore speculate that the local cell-wall architecture provides the cue for Rod-complex initiation, either through direct binding by PBP2 or through an unknown intermediate.
    Keywords cell-wall insertion ; single-enzyme dynamics ; MreB cytoskeleton ; bacterial morphogenesis ; Rod complex ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2020-02-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: A CRISPRi screen in E. coli reveals sequence-specific toxicity of dCas9

    Lun Cui / Antoine Vigouroux / François Rousset / Hugo Varet / Varun Khanna / David Bikard

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 10

    Abstract: CRISPR interference (CRISPRi) is a method for targeted silencing of transcription that requires the coexpression of protein dCas9 and a customized guide RNA. Here, Cui et al. show that certain guide RNAs induce toxicity in E. coli, and provide design ... ...

    Abstract CRISPR interference (CRISPRi) is a method for targeted silencing of transcription that requires the coexpression of protein dCas9 and a customized guide RNA. Here, Cui et al. show that certain guide RNAs induce toxicity in E. coli, and provide design rules to minimize off-target effects.
    Keywords Science ; Q
    Language English
    Publishing date 2018-05-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: A CRISPRi screen in E. coli reveals sequence-specific toxicity of dCas9

    Lun Cui / Antoine Vigouroux / François Rousset / Hugo Varet / Varun Khanna / David Bikard

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 10

    Abstract: CRISPR interference (CRISPRi) is a method for targeted silencing of transcription that requires the coexpression of protein dCas9 and a customized guide RNA. Here, Cui et al. show that certain guide RNAs induce toxicity in E. coli, and provide design ... ...

    Abstract CRISPR interference (CRISPRi) is a method for targeted silencing of transcription that requires the coexpression of protein dCas9 and a customized guide RNA. Here, Cui et al. show that certain guide RNAs induce toxicity in E. coli, and provide design rules to minimize off-target effects.
    Keywords Science ; Q
    Language English
    Publishing date 2018-05-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects

    Antoine Vigouroux / Baptiste Cordier / Andrey Aristov / Laura Alvarez / Gizem Özbaykal / Thibault Chaze / Enno Rainer Oldewurtel / Mariette Matondo / Felipe Cava / David Bikard / Sven van Teeffelen

    eLife, Vol

    2020  Volume 9

    Abstract: Cell shape and cell-envelope integrity of bacteria are determined by the peptidoglycan cell wall. In rod-shaped Escherichia coli, two conserved sets of machinery are essential for cell-wall insertion in the cylindrical part of the cell: the Rod complex ... ...

    Abstract Cell shape and cell-envelope integrity of bacteria are determined by the peptidoglycan cell wall. In rod-shaped Escherichia coli, two conserved sets of machinery are essential for cell-wall insertion in the cylindrical part of the cell: the Rod complex and the class-A penicillin-binding proteins (aPBPs). While the Rod complex governs rod-like cell shape, aPBP function is less well understood. aPBPs were previously hypothesized to either work in concert with the Rod complex or to independently repair cell-wall defects. First, we demonstrate through modulation of enzyme levels that aPBPs do not contribute to rod-like cell shape but are required for mechanical stability, supporting their independent activity. By combining measurements of cell-wall stiffness, cell-wall insertion, and PBP1b motion at the single-molecule level, we then present evidence that PBP1b, the major aPBP, contributes to cell-wall integrity by repairing cell wall defects.
    Keywords peptidoglycan cell wall ; cell envelope ; cell-wall repair ; CRISPRi ; single-molecule tracking ; penicillin-binding proteins ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Computer vision for pattern detection in chromosome contact maps

    Cyril Matthey-Doret / Lyam Baudry / Axel Breuer / Rémi Montagne / Nadège Guiglielmoni / Vittore Scolari / Etienne Jean / Arnaud Campeas / Philippe Henri Chanut / Edgar Oriol / Adrien Méot / Laurent Politis / Antoine Vigouroux / Pierrick Moreau / Romain Koszul / Axel Cournac

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 11

    Abstract: Chromatin loops bridging distant loci within chromosomes can be detected by a variety of techniques such as Hi-C. Here the authors present Chromosight, an algorithm applied on mammalian, bacterial, viral and yeast genomes, able to detect various types of ...

    Abstract Chromatin loops bridging distant loci within chromosomes can be detected by a variety of techniques such as Hi-C. Here the authors present Chromosight, an algorithm applied on mammalian, bacterial, viral and yeast genomes, able to detect various types of pattern in chromosome contact maps, including chromosomal loops.
    Keywords Science ; Q
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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