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dc.contributor.author
Bedez, Claire
dc.contributor.author
Lotz, Christophe
dc.contributor.author
Batisse, Claire
dc.contributor.author
Broeck, Arnaud Vanden
dc.contributor.author
Stote, Roland H.
dc.contributor.author
Howard, Eduardo Ignacio
dc.contributor.author
Pradeau-Aubreton, Karine
dc.contributor.author
Ruff, Marc
dc.contributor.author
Lamour, Valérie
dc.date.available
2019-11-20T16:39:51Z
dc.date.issued
2018-12
dc.identifier.citation
Bedez, Claire; Lotz, Christophe; Batisse, Claire; Broeck, Arnaud Vanden; Stote, Roland H.; et al.; Post-translational modifications in DNA topoisomerase 2α highlight the role of a eukaryote-specific residue in the ATPase domain; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018
dc.identifier.issn
2045-2322
dc.identifier.uri
http://hdl.handle.net/11336/89288
dc.description.abstract
Type 2 DNA topoisomerases (Top2) are critical components of key protein complexes involved in DNA replication, chromosome condensation and segregation, as well as gene transcription. The Top2 were found to be the main targets of anticancer agents, leading to intensive efforts to understand their functional and physiological role as well as their molecular structure. Post-translational modifications have been reported to influence Top2 enzyme activities in particular those of the mammalian Top2α isoform. In this study, we identified phosphorylation, and for the first time, acetylation sites in the human Top2α isoform produced in eukaryotic expression systems. Structural analysis revealed that acetylation sites are clustered on the catalytic domains of the homodimer while phosphorylation sites are located in the C-terminal domain responsible for nuclear localization. Biochemical analysis of the eukaryotic-specific K168 residue in the ATPase domain shows that acetylation affects a key position regulating ATP hydrolysis through the modulation of dimerization. Our findings suggest that acetylation of specific sites involved in the allosteric regulation of human Top2 may provide a mechanism for modulation of its catalytic activity.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Nature Publishing Group
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
DNA TOPOISOMERASE 2α
dc.subject
POST-TRANSLATIONAL MODIFICATIONS
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Post-translational modifications in DNA topoisomerase 2α highlight the role of a eukaryote-specific residue in the ATPase domain
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-17T20:14:16Z
dc.journal.volume
8
dc.journal.number
1
dc.journal.pais
Países Bajos
dc.description.fil
Fil: Bedez, Claire. Université de Strasbourg; Francia
dc.description.fil
Fil: Lotz, Christophe. Université de Strasbourg; Francia
dc.description.fil
Fil: Batisse, Claire. Université de Strasbourg; Francia
dc.description.fil
Fil: Broeck, Arnaud Vanden. Université de Strasbourg; Francia
dc.description.fil
Fil: Stote, Roland H.. Université de Strasbourg; Francia
dc.description.fil
Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
dc.description.fil
Fil: Pradeau-Aubreton, Karine. Université de Strasbourg; Francia
dc.description.fil
Fil: Ruff, Marc. Université de Strasbourg; Francia
dc.description.fil
Fil: Lamour, Valérie. Université de Strasbourg; Francia
dc.journal.title
Scientific Reports
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41598-018-27606-8
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1038/s41598-018-27606-8
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