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dc.contributor.authorHEGNER, MARTIN
dc.date.accessioned2010-04-22T15:53:42Z
dc.date.available2010-04-22T15:53:42Z
dc.date.issued2008
dc.date.submitted2008en
dc.identifier.citationGrange, W., Duckely, M., Husale, S., Jacob,S., Engel, A., Hegner, M., VirE2: A Unique ssDNA Compacting Molecular Machine, PLoS Biology, 6, 2, 2008, 343-351en
dc.identifier.otherY
dc.identifier.urihttp://hdl.handle.net/2262/39179
dc.descriptionPUBLISHEDen
dc.description.abstractThe translocation of single-stranded DNA (ssDNA) across membranes of two cells is a fundamental biological process occurring in both bacterial conjugation and Agrobacterium pathogenesis. Whereas bacterial conjugation spreads antibiotic resistance, Agrobacterium facilitates efficient interkingdom transfer of ssDNA from its cytoplasm to the host plant cell nucleus. These processes rely on the Type IV secretion system (T4SS), an active multiprotein channel spanning the bacterial inner and outer membranes. T4SSs export specific proteins, among them relaxases, which covalently bind to the 5' end of the translocated ssDNA and mediate ssDNA export. In Agrobacterium tumefaciens, another exported protein-VirE2-enhances ssDNA transfer efficiency 2000-fold. VirE2 binds cooperatively to the transferred ssDNA (T-DNA) and forms a compact helical structure, mediating T-DNA import into the host cell nucleus. We demonstrated-using single-molecule techniques-that by cooperatively binding to ssDNA, VirE2 proteins act as a powerful molecular machine. VirE2 actively pulls ssDNA and is capable of working against 50-pN loads without the need for external energy sources. Combining biochemical and cell biology data, we suggest that, in vivo, VirE2 binding to ssDNA allows an efficient import and pulling of ssDNA into the host. These findings provide a new insight into the ssDNA translocation mechanism from the recipient cell perspective. Efficient translocation only relies on the presence of ssDNA binding proteins in the recipient cell that compacts ssDNA upon binding. This facilitated transfer could hence be a more general ssDNA import mechanism also occurring in bacterial conjugation and DNA uptake processes.en
dc.description.sponsorshipSupported by the Swiss National Center of Competence in Research ?Nanoscale Science?, the Swiss National Science Foundation (grant numbers 3152A0?1059531 to M.H. and 3100?059415 to AE), the Maurice E. Muller Foundation of Switzerland, the G.H. Endress foundation, the ELTEM Regio network and the CRANN Science Foundation Ireland.en
dc.format.extent343-351en
dc.language.isoenen
dc.relation.ispartofseriesPLoS Biology;
dc.relation.ispartofseries6;
dc.relation.ispartofseries2;
dc.rightsYen
dc.subjectPhysics
dc.titleVirE2: A Unique ssDNA Compacting Molecular Machineen
dc.typeJournal Articleen
dc.contributor.sponsorScience Foundation Ireland
dc.contributor.sponsorNational Science Foundation
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/hegnerm
dc.identifier.rssinternalid64921


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