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dc.contributor.author
Fernandez, Maricruz
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dc.contributor.author
Shkumatov, Alexander V.
dc.contributor.author
Liu, Yun
dc.contributor.author
Stulemeijer, Claire
dc.contributor.author
Derclaye, Sylvie
dc.contributor.author
Efremov, Rouslan G.
dc.contributor.author
Hallet, Bernard
dc.contributor.author
Alsteens, David
dc.date.available
2024-03-11T11:13:14Z
dc.date.issued
2023-04
dc.identifier.citation
Fernandez, Maricruz; Shkumatov, Alexander V.; Liu, Yun; Stulemeijer, Claire; Derclaye, Sylvie; et al.; AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements; Oxford University Press; Nucleic Acids Research; 51; 10; 4-2023; 4929-4941
dc.identifier.issn
0305-1048
dc.identifier.uri
http://hdl.handle.net/11336/229930
dc.description.abstract
Transposon Tn4430 belongs to a widespread family of bacterial transposons, the Tn3 family, whichplays a prevalent role in the dissemination of antibiotic resistance among pathogens. Despite recentdata on the structural architecture of the transposition complex, the molecular mechanisms underlyingthe replicative transposition of these elements arestill poorly understood. Here, we use force-distancecurve-based atomic force microscopy to probe thebinding of the TnpA transposase of Tn4430 to DNAmolecules containing one or two transposon endsand to extract the thermodynamic and kinetic parameters of transposition complex assembly. Comparing wild-type TnpA with previously isolated deregulated TnpA mutants supports a stepwise pathwayfor transposition complex formation and activationduring which TnpA first binds as a dimer to a single transposon end and then undergoes a structuraltransition that enables it to bind the second end cooperatively and to become activated for transpositioncatalysis, the latter step occurring at a much fasterrate for the TnpA mutants. Our study thus providesan unprecedented approach to probe the dynamic ofa complex DNA processing machinery at the singleparticle level.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Oxford University Press
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
TRANSPOSITION
dc.subject
PROTEIN-DNA INTERACTION
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DYNAMIC FORCE SPECTROSCOPY
dc.subject
AFM
dc.subject.classification
Biofísica
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-03-08T14:48:47Z
dc.identifier.eissn
1362-4962
dc.journal.volume
51
dc.journal.number
10
dc.journal.pagination
4929-4941
dc.journal.pais
Reino Unido
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dc.description.fil
Fil: Fernandez, Maricruz. Université Catholique de Louvain; Bélgica. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados; Argentina
dc.description.fil
Fil: Shkumatov, Alexander V.. Faculty Of Sciences And Bioengineering Sciences ; Vrije Universiteit Brussel;
dc.description.fil
Fil: Liu, Yun. Faculty Of Sciences And Bioengineering Sciences ; Vrije Universiteit Brussel;
dc.description.fil
Fil: Stulemeijer, Claire. Université Catholique de Louvain; Bélgica
dc.description.fil
Fil: Derclaye, Sylvie. Université Catholique de Louvain; Bélgica
dc.description.fil
Fil: Efremov, Rouslan G.. Faculty Of Sciences And Bioengineering Sciences ; Vrije Universiteit Brussel;
dc.description.fil
Fil: Hallet, Bernard. Université Catholique de Louvain; Bélgica
dc.description.fil
Fil: Alsteens, David. Université Catholique de Louvain; Bélgica
dc.journal.title
Nucleic Acids Research
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkad241/7110757
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1093/nar/gkad241
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