PreprintCited by 1Plant Molecular Biology ResearchEpigenetics and DNA MethylationChromosomal and Genetic Variations

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

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Preprint — published as 10.1111/nph.71172

Abstract

PWWP-Domain Interactor of Polycombs 1 (PWO1), also known as PWWP1, interacts with the catalytic subunits of the Polycomb Repressive Complex 2 (PRC2) and, together with PWO2/3 proteins, plays a critical role in the development of Arabidopsis thaliana (At). PWOs are unique to plants and impact chromatin structure by enabling crosstalk between active and repressive epigenetic marks through mechanisms that are not yet fully understood. We aimed to understand the evolution of PWO proteins and whether their interaction with PRC2 has been conserved through evolution. Our study reveals that PWO proteins are present in vascular plants, but absent in bryophytes and green algae. The ancestral clade of PWO proteins includes the Selaginella moellendorffii (Sm) PWO orthologs SmPWOa and SmPWOb. Transient expression assays showed that both AtPWO1 and SmPWOa form nuclear speckles where they tether At, Sm, but also Physcomitrium patens (Pp) PRC2 catalytic subunits, despite the absence of PWO proteins in Pp. The PWO-PRC2 interactions were confirmed by protein-protein analyses. A newly identified evolutionarily conserved short C-terminal alpha-helix (c-motif) in PWO proteins contributes to an interaction interface for PWO-PRC2 binding. SmPWOs partially rescue the pwo1;pwo2 mutant phenotype in Arabidopsis, highlighting the functional conservation of PWOs in vascular plants.

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Metadata

Authors
Khan, A., Haider, S., Sharaf, A., Kusová, A., Skalák, J., Jourdain, C., Rennie, M., Schrumpfová, P. P., Hejátko, J., Schubert, D., Farrona, S., & Mozgová, I.
Affiliations
  • Czech Academy of Sciences (CZ)
  • Ollscoil na Gaillimhe – University of Galway (IE)
  • Central European Institute of Technology (CZ)
  • Freie Universität Berlin (DE)
  • University of Glasgow (GB)
Corresponding author
  • Farrona, Sara
  • Mozgová, Iva
Venue
New Phytologist
Publisher
openRxiv
Published
2025-03-17
Volume
250
Issue
6
Pages
4002-4021
ISSN
0028-646X (ISSN-L)
OpenAlex
W4408608525
Cited by
1
References
2
Citations by year
2025: 1
FWCI
0.00
Type
journal article
Language
en
Open access
Locations
  • New Phytologist (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion, cc-by-sa)
  • Refubium (Universitätsbibliothek der Freien Universität Berlin) (submittedVersion, cc-by)
  • Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver (cc-by)
Funders
  • Ministerstvo Školství, Mládeže a Tělovýchovy (CZ.02.01.01/ 00/22_008/0004581, INTER‐COST LUC24056)
  • Grantová Agentura České Republiky (GA21-15841S, 20/FFP‐P/8693)
  • Akademie Věd České Republiky (CZ.02.01, ERC200961901)
  • Freie Universität Berlin
  • Rheinische Friedrich-Wilhelms-Universität Bonn
  • European Regional Development Fund (CZ.02, CZ.02.01, CZ.02.01.01/00/22_008/0004581)
  • H2020 Marie Skłodowska-Curie Actions (MSCA-IF-2020)
  • Research Ireland
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Chromosomal and Genetic Variations
Keywords
polycomb repressive complex 2, protein evolution, vascular plants, Selaginella moellendorffii, Arabidopsis thaliana, bryophytes, histone methyltransferase, transcriptional silencing, epigenetic regulation, protein-protein interaction, phylogenetic analysis
MeSH terms
Amino Acid Sequence, Phylogeny, Plant Proteins, Protein Binding, Arabidopsis, Evolution, Molecular, Arabidopsis Proteins, Selaginellaceae, Polycomb Repressive Complex 2

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