7O6W

Crystal structure of (the) VEL1 VEL polymerising domain (I664D mutant)

7O6W の概要

• エントリーDOI: 10.2210/pdb7o6w/pdb
• 分子名称: VIN3-like protein 2, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: protein oligomerization, head-to-tail polymerization, nuclear protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16351.48

構造登録者

Fiedler, M.,Franco-Echevarria, E.,Dean, C.,Bienz, M. (登録日: 2021-04-12, 公開日: 2022-11-09, 最終更新日: 2024-06-19)

主引用文献

Fiedler, M.,Franco-Echevarria, E.,Schulten, A.,Nielsen, M.,Rutherford, T.J.,Yeates, A.,Ahsan, B.,Dean, C.,Bienz, M.
Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control.
Cell Rep, 41:111607-111607, 2022

PubMed Abstract: Transcriptional silencing through the Polycomb silencing machinery utilizes a "read-write" mechanism involving histone tail modifications. However, nucleation of silencing and long-term stable transmission of the silenced state also requires P-olycomb Repressive Complex 2 (PRC2) accessory proteins, whose molecular role is poorly understood. The Arabidopsis VEL proteins are accessory proteins that interact with PRC2 to nucleate and propagate silencing at the FLOWERING LOCUS C (FLC) locus, enabling early flowering in spring. Here, we report that VEL proteins contain a domain related to an atypical four-helix bundle that engages in spontaneous concentration-dependent head-to-tail polymerization to assemble dynamic biomolecular condensates. Mutations blocking polymerization of this VEL domain prevent Polycomb silencing at FLC. Plant VEL proteins thus facilitate assembly of dynamic multivalent Polycomb complexes required for inheritance of the silenced state.

PubMed: 36351412
DOI: 10.1016/j.celrep.2022.111607

実験手法

X-RAY DIFFRACTION (2.64 Å)