Authors: | Wang, H.; Cao, R.; Xia, L.; Erdjument-Bromage, H.; Borchers, C.; Tempst, P.; Zhang, Y. |
Article Title: | Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase |
Abstract: | 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. |
Keywords: | controlled study; unclassified drug; human cell; methylation; protein domain; protein function; protein analysis; animals; cell cycle proteins; mice; hela cell; hela cells; transcription factors; methyltransferases; transcription regulation; amino acid sequence; molecular sequence data; protein purification; histone-lysine n-methyltransferase; molecular recognition; nucleotide sequence; histone h3; substrate specificity; protein structure, tertiary; gene silencing; molecular weight; histones; protein derivative; lysine; acetyltransferases; protein methylation; heterochromatin; acetylation; dna, complementary; nucleosomes; histone lysine methyltransferase; protein p300; binding, competitive; histone acetyltransferases; humans; human; article; protein set7; protein suv39h1 |
Journal Title: | Molecular Cell |
Volume: | 8 |
Issue: | 6 |
ISSN: | 1097-2765 |
Publisher: | Cell Press |
Date Published: | 2001-12-01 |
Start Page: | 1207 |
End Page: | 1217 |
Language: | English |
DOI: | 10.1016/s1097-2765(01)00405-1 |
PUBMED: | 11779497 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Export Date: 21 May 2015 -- Source: Scopus |