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Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity.

Abstract：

:Evolutionary conserved SET domains were originally identified in three Drosophila proteins: suppressor of variegation (Su (var) 3-9), enhancer of zeste (E(z)), and the trithorax. Some of the SET-domain containing proteins have been known to elicit methylation of histone lysine residues. Based on a search for SET-domain containing proteins using bioinformatic tools, we identified and subsequently named a novel SET domain as WHISTLE, that has histone methyltransferase (HMTase) activity. To characterize WHISTLE, we performed an HMTase assay, mass spectrometric analysis, lysine specificity, and transfection assays. Mass spectrometric and immunoblot analysis revealed that WHISTLE di-methylates H3K4 and di-, and tri-methylates H3K27 of histones. Overexpression of WHISTLE repressed transcription of the SV40 promoter. Our results suggest that WHISTLE is a novel SET domain containing a protein with specific H3K4 and H3K27 HMTase activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kim SM,Kee HJ,Eom GH,Choe NW,Kim JY,Kim YS,Kim SK,Kook H,Kook H,Seo SB

doi

10.1016/j.bbrc.2006.04.095

subject

Has Abstract

pub_date

2006-06-23 00:00:00

pages

318-23

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00939-9

journal_volume

345

pub_type

杂志文章

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