Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation

J Biol Chem. 2010 Mar 26;285(13):9322-9326. doi: 10.1074/jbc.C109.097667.

Hong Wen ¹, Jingzhi Li ², Tanjing Song ¹, Ming Lu ³, Pu-Yeh Kan ⁴, Min Gyu Lee ⁴, Bingdong Sha ², Xiaobing Shi ⁵

Affiliations

1 Departments of Biochemistry and Molecular Biology, Houston, Texas 77030; Centers for Cancer Epigenetics, Houston, Texas 77030; Stem Cell and Developmental Biology, Houston, Texas 77030.
2 Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35205.
3 Departments of Biochemistry and Molecular Biology, Houston, Texas 77030.
4 Centers for Cancer Epigenetics, Houston, Texas 77030; Molecular and Cellular Oncology, Houston, Texas 77030.
5 Departments of Biochemistry and Molecular Biology, Houston, Texas 77030; Centers for Cancer Epigenetics, Houston, Texas 77030; Stem Cell and Developmental Biology, Houston, Texas 77030; Genes and Development Graduate Program, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030. Electronic address: xbshi@mdanderson.org.

PMID: 20129925 DOI: 10.1074/jbc.C109.097667

Abstract

Distinct lysine methylation marks on histones create dynamic signatures deciphered by the "effector" modules, although the underlying mechanisms remain unclear. We identified the plant homeodomain- and Jumonji C domain-containing protein PHF2 as a novel histone H3K9 demethylase. We show in biochemical and crystallographic analyses that PHF2 recognizes histone H3K4 trimethylation through its plant homeodomain finger and that this interaction is essential for PHF2 occupancy and H3K9 demethylation at rDNA promoters. Our study provides molecular insights into the mechanism by which distinct effector domains within a protein cooperatively modulate the "cross-talk" of histone modifications.

Name
Email *

	Sorry, but the email address you supplied was invalid.