Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold

被引：32

作者：

Dlakic, M ^{[1
]}

机构：

[1] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2001年 / 26卷 / 07期

关键词：

D O I：

10.1016/S0968-0004(01)01856-4

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：

Although protein methylation has been observed for decades, its functional significance has remained largely unclear. Using sensitive profile searches and structural modeling, chromatin silencing protein and meiotic recombination checkpoint regulator Dot1p was identified as a putative protein methyltransferase. Along with recent results that link histone H3 methylation with chromatin silencing, this finding suggests that an expanded combinatorial repertoire of protein modifications affects transcriptional regulation.

引用

页码：405 / 407

页数：3

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