All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

PWO proteins are associated with PRC2 since their emergence in vascular plants

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F26%3A00144778" target="_blank" >RIV/00216224:14740/26:00144778 - isvavai.cz</a>

  • Result on the web

    <a href="https://nph.onlinelibrary.wiley.com/doi/10.1111/nph.71172" target="_blank" >https://nph.onlinelibrary.wiley.com/doi/10.1111/nph.71172</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1111/nph.71172" target="_blank" >10.1111/nph.71172</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    PWO proteins are associated with PRC2 since their emergence in vascular plants

  • Original language description

    The Polycomb repressive complex 2 (PRC2), a conserved histone methyltransferase complex, plays a central role in transcriptional silencing across eukaryotes. Here, we investigate the evolution of PWWP-DOMAIN INTERACTORS OF POLYCOMBS (PWOs), which interact with PRC2, and examine the conservation of the PWOs-PRC2 interaction across plant evolution by comparing orthologs from the lycophyte Selaginella moellendorffii (Sm) and the flowering plant Arabidopsis thaliana (Arabidopsis; At). Phylogenetic data traced the presence of PWO proteins across plant lineages, while protein-protein interaction assays and AlphaFold predictions assessed PWO-PRC2 interactions and structural conservation. Functional complementation assays confirmed PWOs' conserved functions. PWO proteins are present in vascular plants but absent in bryophytes and green algae. The ancestral clade of PWO proteins includes the spikemoss Selaginella moellendorffii (Sm) PWO orthologs SmPWOa and SmPWOb. PWO proteins from vascular plants can interact with PRC2 components from multiple species, including bryophytes, which naturally lack PWOs. The PWO-PRC2 interaction is mediated by a conserved short C-motif. Functional and molecular assays further demonstrate that SmPWOs retain their conserved functions in Arabidopsis. Our data suggest an evolutionarily conserved role for PWOs in modulating PRC2 activity and emphasize how lineage-specific proteins associated with conserved chromatin-modifying complexes may shape epigenetic control mechanisms during evolution.

  • Czech name

    —

  • Czech description

    —

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

    —

  • OECD FORD branch

    10611 - Plant sciences, botany

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2026

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    NEW PHYTOLOGIST

  • ISSN

    0028-646X

  • e-ISSN

    1469-8137

  • Volume of the periodical

    250

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    20

  • Pages from-to

    4002-4021

  • UT code for WoS article

    001744307700001

  • EID of the result in the Scopus database

    2-s2.0-105036291511