Putting the Pieces Together: Histone H2B Ubiquitylation Directly Stimulates Histone H3K79 Methylation

被引：3

作者：

Jeltsch, Albert ^{[1
]}

Rathert, Philipp ^{[1
]}

机构：

[1] Jacobs Univ Bremen, Sch Sci & Engn, Biochem Lab, D-28759 Bremen, Germany

来源：

CHEMBIOCHEM | 2008年 / 9卷 / 14期

关键词：

enzymes; histone; methylation; nucleosomes; ubiquitylation;

D O I：

10.1002/cbic.200800414

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：

Employing an in vitro reconstruction approach, McGinty et al. studied the mechanism of stimulation of the Dot1-catalysed histone H3 methylation at Lys79 by histone H2B ubiquitylation at Lys120. To generate nucleosome particles that carry the uniquitylation at Lys120, they chemically connected three polypeptides the main parts of histone He and ubiquitin expressed in bacteria and a branched synthetic peptide. Using the semisynthetically produced nucleosome substrates and purified Dot1 enzyme, they showed that Dot1 is directly stimulated by the ubiquitylation, thus ruling out the need for further protein factorss to mediate the effect.

引用

页码：2193 / 2195

页数：3

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