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KDM2A integrates DNA and histone modification signals through a CXXC/PHD module and direct interaction with HP1.

Abstract：

:Functional genomic elements are marked by characteristic DNA and histone modification signatures. How combinatorial chromatin modification states are recognized by epigenetic reader proteins and how this is linked to their biological function is largely unknown. Here we provide a detailed molecular analysis of chromatin recognition by the lysine demethylase KDM2A. Using biochemical approaches we identify a nucleosome interaction module within KDM2A consisting of a CXXC type zinc finger, a PHD domain and a newly identified Heterochromatin Protein 1 (HP1) interaction motif that mediates direct binding between KDM2A and HP1. This nucleosome interaction module enables KDM2A to decode nucleosomal H3K9me3 modification in addition to CpG methylation signals. The multivalent engagement with DNA and HP1 results in a nucleosome binding circuit in which KDM2A can be recruited to H3K9me3-modified chromatin through HP1, and HP1 can be recruited to unmodified chromatin by KDM2A. A KDM2A mutant deficient in HP1-binding is inactive in an in vivo overexpression assay in zebrafish embryos demonstrating that the HP1 interaction is essential for KDM2A function. Our results reveal a complex regulation of chromatin binding for both KDM2A and HP1 that is modulated by DNA- and H3K9-methylation, and suggest a direct role for KDM2A in chromatin silencing.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Borgel J,Tyl M,Schiller K,Pusztai Z,Dooley CM,Deng W,Wooding C,White RJ,Warnecke T,Leonhardt H,Busch-Nentwich EM,Bartke T

doi

10.1093/nar/gkw979

subject

Has Abstract

pub_date

2017-02-17 00:00:00

pages

1114-1129

issue

3

eissn

0305-1048

issn

1362-4962

pii

2290933

journal_volume

45

pub_type

杂志文章

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