Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase

被引：446

作者：

Wang, HB

Cao, R

Xia, L

Erdjument-Bromage, H

Borchers, C

Tempst, P

Zhang, Y ^{[1
]}

机构：

[1] Univ N Carolina, Dept Biochem & Biophys, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA

[2] Mem Sloan Kettering Canc Ctr, Program Mol Biol, New York, NY 10021 USA

来源：

MOLECULAR CELL | 2001年 / 8卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(01)00405-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Methylation of histone H3 at lysine 9 by SUV39H1 and subsequent recruitment of the heterochromatin protein HPI has recently been linked to gene silencing. In addition to lysine 9, histone H3 methylation also occurs at lysines 4, 27, and 36. Here, we report the purification, molecular identification, and functional characterization of an H3-lysine 4-specific methyltransferase (H3-K4-HMTase), SET7. We demonstrate that SET7 methylates H3-K4 in vitro and in vivo. In addition, we found that methylation of H3-K4 and H3-K9 inhibit each other. Furthermore, H3-K4 and H3-K9 methylation by SET7 and SUV39H1, respectively, have differential effects on subsequent histone acetylation by p300. Thus, our study provides a molecular explanation to the differential effects of H3-K4 and H3-K9 methylation on transcription.

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页码：1207 / 1217

页数：11

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