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

Hengbin Wang, Ru Cao, Li Xia, Hediye Erdjument-Bromage, Christoph Borchers, Paul Tempst, Yi Zhang

Research output: Contribution to journalArticlepeer-review

437 Citations (Scopus)


Methylation of histone H3 at lysine 9 by SUV39H1 and subsequent recruitment of the heterochromatin protein HP1 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.

Original languageEnglish
Pages (from-to)1207-1217
Number of pages11
JournalMolecular Cell
Issue number6
Publication statusPublished - 2001
Externally publishedYes


Dive into the research topics of 'Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase'. Together they form a unique fingerprint.

Cite this