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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control Marc Fiedler , Elsa Franco-Echevarria , Anna Schulten , Mathias Nielsen , Trevor J. Rutherford , Anna Yeates , Bilal Ahsan , Caroline Dean , Mariann Bienz Cell Reports 41 DOI: 10.1016/j.celrep.2022.111607 Diamond Proposal Number(s): [21426] Open Access Show Abstract ▼ 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.	Nov 2022

Instruments / Technical Area

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I04-Macromolecular Crystallography
I24-Microfocus Macromolecular Crystallography

Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control

Marc Fiedler , Elsa Franco-Echevarria , Anna Schulten , Mathias Nielsen , Trevor J. Rutherford , Anna Yeates , Bilal Ahsan , Caroline Dean , Mariann Bienz

Cell Reports 41

DOI: 10.1016/j.celrep.2022.111607

Diamond Proposal Number(s): [21426]