(7/n)
Overall, this is a first study of its kind that explores the PWO-PRC2 interaction and how PWOs might have contributed to PRC2 evolution in vascular plants.

(6/n)
Finally, we introduced SmPWOs (SmPWOa and SmPWOb) in At pwo1, pwo2 mutants as a way to analyze if representative of ancestral PWOs could complement the defects in At. Interestingly, SmPWOa could partially complement all the defects observed in At pwo1:pwo2 mutants.

(5/n)
Further, PWOs from At and Sm could interact with moss PRC2 components, despite the absence of PWOs in Physcomitrella patens. Next, a short C-terminal motif was identified in PWOs, which is proposed to provide/ contribute to an interaction interface for PWO-PRC2 binding.

(4/n)
As a representative of ancestral PWOs, we worked on Selaginella moellendorffii (Sm) PWOs (SmPWOa/b) and showed their interaction with Arabidopsis thaliana (At) PRC2 catalytic subunits (SWN/CLF).

(3/n)
PWOs have been proposed to play a role in transcriptional activation as well as repression through their association with PEAT and PRC2 complexes. To better understand the PWO-PRC2 interaction, a range of PPI studies were conducted, including Y2H, BiFC, and FLIM-FRET.

(2/n)
Unlike PRC2 components that are present in all plants, PWOs are absent in lower plants (Green algae and Bryophytes) and first emerged in vascular plants, i.e., Lycophytes (Selaginella moellendorffii), coinciding with the transition to land