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Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.
Autor:
Prince JP; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; Meiosis Group, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London, W12 0NN, UK., Bolla JR; Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.; The Kavli Institute for Nanoscience Discovery, South Parks Road, Oxford, OX1 3QU, UK.; Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Fisher GLM; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; DNA Motors Group, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London, W12 0NN, UK., Mäkelä J; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; ChEM-H Institute, Stanford University, 290 Jane Stanford Way, Stanford, CA, 94305, USA., Fournier M; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Robinson CV; Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.; The Kavli Institute for Nanoscience Discovery, South Parks Road, Oxford, OX1 3QU, UK., Arciszewska LK; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Sherratt DJ; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. david.sherratt@bioch.ox.ac.uk.
Publikováno v:
Nature communications [Nat Commun] 2021 Nov 18; Vol. 12 (1), pp. 6721. Date of Electronic Publication: 2021 Nov 18.
Autor:
Fisher GL; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Bolla JR; Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, United Kingdom.; The Kavli Institute for Nanoscience Discovery, Oxford, United Kingdom., Rajasekar KV; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Mäkelä J; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Baker R; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Zhou M; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Prince JP; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Stracy M; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Robinson CV; Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, United Kingdom.; The Kavli Institute for Nanoscience Discovery, Oxford, United Kingdom., Arciszewska LK; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Sherratt DJ; Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Publikováno v:
ELife [Elife] 2021 Sep 29; Vol. 10. Date of Electronic Publication: 2021 Sep 29.
Autor:
Mäkelä J; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom david.sherratt@bioch.ox.ac.uk jmakela@stanford.edu., Uphoff S; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Sherratt DJ; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom david.sherratt@bioch.ox.ac.uk jmakela@stanford.edu.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Aug 17; Vol. 118 (33).
Xer-mediated dimer resolution at the mwr site of the multiresistance plasmid pJHCMW1 is osmoregulated in Escherichia coli containing either the Escherichia coli Xer recombination machinery or Xer recombination elements from K. pneumoniae. In the pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::494775777148f02b7a697a1ccc0b896e
https://doi.org/10.1128/jb.188.8.2812-2820.2006
https://doi.org/10.1128/jb.188.8.2812-2820.2006
Site-specific recombinases XerC and XerD function in the segregation of circular bacterial replicons. In a recombining nucleoprotein complex containing two molecules each of XerC and XerD, coordinated reciprocal switches in recombinase activity ensur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::da28e886ff31f2db77c6cc6085df3fe6
https://doi.org/10.1006/jmbi.2000.3762
https://doi.org/10.1006/jmbi.2000.3762
Chromosome dimers form in bacteria by recombination between circular chromosomes. Resolution of dimers is a highly integrated process involving recombination between dif sites catalysed by the XerCD recombinase, cell division and the integrity of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b48fbf8dbbaac50a575f88e017ba8b24
https://doi.org/10.1046/j.1365-2958.2001.02277.x
https://doi.org/10.1046/j.1365-2958.2001.02277.x
In Xer site-specific recombination, sequential DNA strand exchange reactions are catalyzed by a heterotetrameric complex composed of two recombinases, XerC and XerD. It is demonstrated that XerC and XerD catalytic activity is controlled by an interac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::70e2d357feb7879bb90d557119e67650
https://ora.ox.ac.uk/objects/uuid:071c9c9b-1f02-4fe8-a0df-f806c0fdb743
https://ora.ox.ac.uk/objects/uuid:071c9c9b-1f02-4fe8-a0df-f806c0fdb743