13 research outputs found

    Weaving Seats and Panels in Furniture

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    Jugendarbeit Wallisellen : Bestandessichtung, Analyse und Empfehlungen - Schlussbericht

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    Das Ressort Gesellschaft der Gemeinde Wallisellen, Kanton Zürich wollte auf der Basis einer externen Bestandessichtung und Analyse sowie eines darauf aufbauenden Konzeptrahmens und entsprechenden Empfehlungen die Weiterentwicklung der Jugendarbeit Wallisellen planen. Die ZHAW, Departement Soziale Arbeit wurde beauftragt, zwischen Dezember 2012 und Mai 2013 die Sichtung und Analyse vorzunehmen und in Berichtsform Konzeptrahmen und Empfehlungen aufzuzeigen. Der ZHAW stand dafür eine ausführliche Bestandesdokumentation – erstellt von der Abteilung Gesellschaft Wallisellen – zur Verfügung. Ergänzend dazu wurden von der ZHAW Interviews mit zehn Schlüsselpersonen der Jugendarbeit Wallisellen geführt. Auf dieser Datenbasis erstellte sie den vorliegenden Bericht.

    Familie und Soziale Arbeit : drei begrifflich-theoretische Konzepte von Familie im Überblick

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    Im August 2015 wird das Institut für Kindheit, Jugend und Familie, Departement Soziale Arbeit, ZHAW gegründet. Drei thematische Schwerpunkte sind für das Institut leitend: (I) Kinder- und Jugendhilfe, (II) Soziale Arbeit und Schule sowie (III) Familie und Aufwachsen. Im Mai 2016 nimmt die Fokusgruppe Familie und Aufwachsen ihre Arbeit auf. Das Studienjahr 2016/2017 ist dem Thema Familie gewidmet. Das vorliegende Working Paper dokumentiert die wichtigsten Ergebnisse der Diskussionen

    Duplex DNA and BLM regulate gate opening by the human TopoIIIα-RMI1-RMI2 complex

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    Topoisomerase IIIα is a type 1A topoisomerase that forms a complex with RMI1 and RMI2 called TRR in human cells. TRR plays an essential role in resolving DNA replication and recombination intermediates, often alongside the helicase BLM. While the TRR catalytic cycle is known to involve a protein-mediated single-stranded (ss)DNA gate, the detailed mechanism is not fully understood. Here, we probe the catalytic steps of TRR using optical tweezers and fluorescence microscopy. We demonstrate that TRR forms an open gate in ssDNA of 8.5 ± 3.8 nm, and directly visualize binding of a second ssDNA or double-stranded (ds)DNA molecule to the open TRR-ssDNA gate, followed by catenation in each case. Strikingly, dsDNA binding increases the gate size (by ~16%), while BLM alters the mechanical flexibility of the gate. These findings reveal an unexpected plasticity of the TRR-ssDNA gate size and suggest that TRR-mediated transfer of dsDNA may be more relevant in vivo than previously believed

    Furniture Arrangment

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    Imaging unlabeled proteins on DNA with super-resolution

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    Fluorescence microscopy is invaluable to a range of biomolecular analysis approaches. The required labeling of proteins of interest, however, can be challenging and potentially perturb biomolecular functionality as well as cause imaging artefacts and photo bleaching issues. Here, we introduce inverse (super-resolution) imaging of unlabeled proteins bound to DNA. In this new method, we use DNA-binding fluorophores that transiently label bare DNA but not protein-bound DNA. In addition to demonstrating diffraction-limited inverse imaging, we show that inverse Binding-Activated Localization Microscopy or 'iBALM' can resolve biomolecular features smaller than the diffraction limit. The current detection limit is estimated to lie at features between 5 and 15 nm in size. Although the current image-acquisition times preclude super-resolving fast dynamics, we show that diffraction-limited inverse imaging can reveal molecular mobility at ∼0.2 s temporal resolution and that the method works both with DNA-intercalating and non-intercalating dyes. Our experiments show that such inverse imaging approaches are valuable additions to the single-molecule toolkit that relieve potential limitations posed by labeling

    Duplex DNA and BLM regulate gate opening by the human TopoIIIα-RMI1-RMI2 complex

    No full text
    Topoisomerase IIIα is a type 1A topoisomerase that forms a complex with RMI1 and RMI2 called TRR in human cells. TRR plays an essential role in resolving DNA replication and recombination intermediates, often alongside the helicase BLM. While the TRR catalytic cycle is known to involve a protein-mediated single-stranded (ss)DNA gate, the detailed mechanism is not fully understood. Here, we probe the catalytic steps of TRR using optical tweezers and fluorescence microscopy. We demonstrate that TRR forms an open gate in ssDNA of 8.5 ± 3.8 nm, and directly visualize binding of a second ssDNA or double-stranded (ds)DNA molecule to the open TRR-ssDNA gate, followed by catenation in each case. Strikingly, dsDNA binding increases the gate size (by ~16%), while BLM alters the mechanical flexibility of the gate. These findings reveal an unexpected plasticity of the TRR-ssDNA gate size and suggest that TRR-mediated transfer of dsDNA may be more relevant in vivo than previously believed
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