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dc.contributor.author
Schmücker, Anna
dc.contributor.author
Lei, Bingkun
dc.contributor.author
Lorkovic, Zdravko J.
dc.contributor.author
Capella, Matias
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dc.contributor.author
Braun, Sigurd
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Bourguet, Pierre
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Mathieu, Olivier
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Mechtler, Karl
dc.contributor.author
Berger, Frédéric
dc.date.available
2023-01-19T14:10:12Z
dc.date.issued
2021-06
dc.identifier.citation
Schmücker, Anna; Lei, Bingkun; Lorkovic, Zdravko J.; Capella, Matias; Braun, Sigurd; et al.; Crosstalk between H2A variant-specific modifications impacts vital cell functions; Public Library of Science; Plos Genetics; 17; 6; 6-2021; 1-27
dc.identifier.issn
1553-7390
dc.identifier.uri
http://hdl.handle.net/11336/185013
dc.description.abstract
Selection of C-terminal motifs participated in evolution of distinct histone H2A variants. Hybrid types of variants combining motifs from distinct H2A classes are extremely rare. This suggests that the proximity between the motif cases interferes with their function. We studied this question in flowering plants that evolved sporadically a hybrid H2A variant combining the SQ motif of H2A.X that participates in the DNA damage response with the KSPK motif of H2A.W that stabilizes heterochromatin. Our inventory of PTMs of H2A.W variants showed that in vivo the cell cycle-dependent kinase CDKA phosphorylates the KSPK motif of H2A. W but only in absence of an SQ motif. Phosphomimicry of KSPK prevented DNA damage response by the SQ motif of the hybrid H2A.W/X variant. In a synthetic yeast expressing the hybrid H2A.W/X variant, phosphorylation of KSPK prevented binding of the BRCT-domain protein Mdb1 to phosphorylated SQ and impaired response to DNA damage. Our findings illustrate that PTMs mediate interference between the function of H2A variant specific C-terminal motifs. Such interference could explain the mutual exclusion of motifs that led to evolution of H2A variants.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Public Library of Science
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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
Histone variants
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Post-translational modifications
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Arabidopsis thaliana
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BRCT domain
dc.subject.classification
Bioquímica y Biología Molecular
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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
Crosstalk between H2A variant-specific modifications impacts vital cell functions
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-09-21T16:17:56Z
dc.journal.volume
17
dc.journal.number
6
dc.journal.pagination
1-27
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Schmücker, Anna. Austrian Academy Of Sciences (oaw);
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Fil: Lei, Bingkun. Austrian Academy Of Sciences (oaw);
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Fil: Lorkovic, Zdravko J.. Ludwig Maximilians Universitat; Alemania
dc.description.fil
Fil: Capella, Matias. Ludwig Maximilians Universitat; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
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Fil: Braun, Sigurd. Ludwig Maximilians Universitat; Alemania
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Fil: Bourguet, Pierre. Gregor Mendel Institute Of Molecular Plant Biology; Austria. Université Clermont Auvergne; Francia
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Fil: Mathieu, Olivier. Université Clermont Auvergne; Francia
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Fil: Mechtler, Karl. Gregor Mendel Institute Of Molecular Plant Biology; Austria
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Fil: Berger, Frédéric. Gregor Mendel Institute Of Molecular Plant Biology; Austria
dc.journal.title
Plos Genetics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1371/journal.pgen.1009601
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