Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
H2A deubiquitinases UBP12/13 are part of the Arabidopsis polycomb group protein system
Show others and affiliations
Number of Authors: 10
2016 (English)In: nature plants, ISSN 2055-026X, Vol. 2, no 9, 16126Article in journal (Refereed) Published
Abstract [en]

Polycomb group (PcG) proteins form an epigenetic memory system in plants and animals, but interacting proteins are poorly known in plants. Here, we have identified Arabidopsis UBIQUITIN SPECIFIC PROTEASES (USP; UBP in plant and yeasts) 12 and 13 as partners of the plant-specific PcG protein LIKE HETEROCHROMATIN PROTEIN 1 (LHP1). UBP12 binds to chromatin of PcG target genes and is required for histone H3 lysine 27 trimethylation and repression of a subset of PcG target genes. Plants lacking UBP12 and UBP13 developed autonomous endosperm in the absence of fertilization. We have identified UBP12 and UBP13 as new proteins in the plant PcG regulatory network. UBP12 and UBP13 belong to an ancient gene family and represent plant homologues of metazoan USP7. We have found that Drosophila USP7 shares a function in heterochromatic gene repression with UBP12/13 and their homologue UBP26. In summary, we demonstrate that USP7-like proteins are essential for gene silencing in diverse genomic contexts.

Place, publisher, year, edition, pages
2016. Vol. 2, no 9, 16126
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-135974DOI: 10.1038/NPLANTS.2016.126ISI: 000385011300003PubMedID: 27525512OAI: oai:DiVA.org:su-135974DiVA: diva2:1050514
Available from: 2016-11-29 Created: 2016-11-28 Last updated: 2016-11-29Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Tang, MinMannervik, Mattias
By organisation
Department of Molecular Biosciences, The Wenner-Gren Institute
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 21 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf