西亚试剂：Heterogeneous Nuclear Ribonucleoprotein L Is a Subunit of H

Heterogeneous Nuclear Ribonucleoprotein L Is a Subunit of Human KMT3a/Set2 Complex Required for H3 Lys-36 Trimethylation Activity in Vivo*

Wen Yuan?1, Jingwei Xie?1, Chengzu Long?, Hediye Erdjument-Bromage||, Xiaojun Ding?, Yong Zheng?**, Paul Tempst||, She Chen?, Bing Zhu?**2, and Danny Reinberg**3

From the From the State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100094, China, the ,  Graduate Program, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100730, China, the , ?National Institute of Biological Sciences, 7 Science Park Road, Zhong Guan Cun Life Science Park, Beijing 102206, China, the , ||Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10021, and the , **Howard Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, New York 10016

ABSTRACT

The presence of histone H3 lysine 36 methylation (H3K36me) correlates with actively transcribed genes. In yeast, histone H3K36me mediated by KMT3 (also known as Set2) recruits a histone deacetylase complex, Rpd3s, to ensure the fidelity of transcription initiation. We report the purification of human KMT3a (also known as HYPB or hSet2) complex and the identification of a novel, higher eukaryotic specific subunit, heterogeneous nuclear ribonucleoprotein L (HnRNP-L). Interestingly, although KMT3a has intrinsic activity in vitro, HnRNP-L is essential in vivo. Moreover, KMT3a generates mono-, di-, and trimethylated products in vitro, but RNA interference against KMT3a or HnRNP-L down-regulates exclusively the H3K36me3 mark in vivo.

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