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A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate transcription at active genes
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A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate transcription at active genes
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Journal Article
A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate transcription at active genes
2018
Overview
Transcriptional regulation by chromatin is a highly dynamic process directed through the recruitment and coordinated action of epigenetic modifiers and readers of these modifications. Using an unbiased proteomic approach to find interactors of H3K36me3, a modification enriched on active chromatin, here we identify PWWP2A and HDAC2 among the top interactors. PWWP2A and its paralog PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66α/β, and CHD3/4. PWWP2A competes with MBD3 for binding to MTA1, thus defining a new variant NuRD complex that is mutually exclusive with the MBD2/3 containing NuRD. In mESCs, PWWP2A/B is most enriched at highly transcribed genes. Loss of PWWP2A/B leads to increases in histone acetylation predominantly at highly expressed genes, accompanied by decreases in Pol II elongation. Collectively, these findings suggest a role for PWWP2A/B in regulating transcription through the fine-tuning of histone acetylation dynamics at actively transcribed genes.
Transcription regulation requires recruitment of different epigenetic regulators to the chromatin. Here the authors provide evidence that an H3K36me3 reader PWWP2A forms a variant NuRD complex and plays a role in regulating transcription and histone acetylation dynamics.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 49/23
/ 82/58
/ 82/80
/ Animals
/ Chromosomal Proteins, Non-Histone - genetics
/ Chromosomal Proteins, Non-Histone - metabolism
/ DNA Methylation - physiology
/ DNA-Binding Proteins - metabolism
/ Genes
/ Humanities and Social Sciences
/ Humans
/ Mi-2 Nucleosome Remodeling and Deacetylase Complex - metabolism
/ Mice
/ RNA Polymerase II - metabolism
/ Science
