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Cryo-EM structure of the full human PRC2 and regulation by AEBP2 and JARID2

ABSTRACT: Structural study of the PRC2 complex and its regulators AEPB2 and JARID2 combining cryo-EM, cross-linking, targeted MS and hydrogen/deuterium exchange MS.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Marco Faini

LAB HEAD: Ruedi Aebersold

PROVIDER: PXD008605 | Pride | 2018-01-25

REPOSITORIES: Pride

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			Action	DRS
	PRC2_A2J2_all_sequences.fasta	Fasta
	Results_summary.xlsx	Xlsx
	mfaini_D1607_170.raw	Raw
	mfaini_D1607_171.raw	Raw
	mfaini_D1607_173.raw	Raw

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Publications

Structures of human PRC2 with its cofactors AEBP2 and JARID2.

Kasinath Vignesh V Faini Marco M Poepsel Simon S Reif Dvir D Feng Xinyu Ashlee XA Stjepanovic Goran G Aebersold Ruedi R Nogales Eva E

Science (New York, N.Y.) 20180118 6378

Transcriptionally repressive histone H3 lysine 27 methylation by Polycomb repressive complex 2 (PRC2) is essential for cellular differentiation and development. Here we report cryo-electron microscopy structures of human PRC2 in a basal state and two distinct active states while in complex with its cofactors JARID2 and AEBP2. Both cofactors mimic the binding of histone H3 tails. JARID2, methylated by PRC2, mimics a methylated H3 tail to stimulate PRC2 activity, whereas AEBP2 interacts with the R ...[more]

PMID: 29348366

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