Completing the TRB family: newly characterized members show ancient evolutionary origins and distinct localization, yet similar interactions

0575345 - ÚEB 2024 RIV DE eng J - Journal Article
Kusová, A. - Steinbachová, Lenka - Přerovská, T. - Záveská Drábková, Lenka - Paleček, J. - Khan, Ahamed - Rigóová, G. - Gadiou, Zuzana - Jourdain, C. - Stricker, T. - Schubert, D. - Honys, David - Schrumpfová, P.
Completing the TRB family: newly characterized members show ancient evolutionary origins and distinct localization, yet similar interactions.
Plant Molecular Biology. Roč. 112, 1-2 (2023), s. 61-83. ISSN 0167-4412. E-ISSN 1573-5028
R&D Projects: GA ČR(CZ) GA21-15841S; GA MŠMT(CZ) LTAUSA18115; GA MŠMT(CZ) LM2018129
Institutional support: RVO:61389030 ; RVO:60077344
Keywords : peat * prc2 * Telomere repeat binding * Telomeric * tert * trb
OECD category: Plant sciences, botany; Plant sciences, botany (BC-A)
Impact factor: 5.1, year: 2022
Method of publishing: Open access
https://doi.org/10.1007/s11103-023-01348-2

Telomere repeat binding proteins (TRBs) belong to a family of proteins possessing a Myb-like domain which binds to telomeric repeats. Three members of this family (TRB1, TRB2, TRB3) from Arabidopsis thaliana have already been described as associated with terminal telomeric repeats (telomeres) or short interstitial telomeric repeats in gene promoters (telo-boxes). They are also known to interact with several protein complexes: telomerase, Polycomb repressive complex 2 (PRC2) E(z) subunits and the PEAT complex (PWOs-EPCRs-ARIDs-TRBs). Here we characterize two novel members of the TRB family (TRB4 and TRB5). Our wide phylogenetic analyses have shown that TRB proteins evolved in the plant kingdom after the transition to a terrestrial habitat in Streptophyta, and consequently TRBs diversified in seed plants. TRB4-5 share common TRB motifs while differing in several others and seem to have an earlier phylogenetic origin than TRB1-3. Their common Myb-like domains bind long arrays of telomeric repeats in vitro, and we have determined the minimal recognition motif of all TRBs as one telo-box. Our data indicate that despite the distinct localization patterns of TRB1-3 and TRB4-5 in situ, all members of TRB family mutually interact and also bind to telomerase/PRC2/PEAT complexes. Additionally, we have detected novel interactions between TRB4-5 and EMF2 and VRN2, which are Su(z)12 subunits of PRC2.
Permanent Link: https://hdl.handle.net/11104/0345131