Tails of intrigue: Phosphorylation of RNA polymerase II mediates histone methylation

被引：255

作者：

Hampsey, M

Reinberg, D ^{[1
]}

机构：

[1] Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Piscataway, NJ 08854 USA

[2] Robert Wood Johnson Med Sch, Dept Biochem, Div Nucl Acids Enzymol, Piscataway, NJ 08854 USA

来源：

CELL | 2003年 / 113卷 / 04期

关键词：

D O I：

10.1016/S0092-8674(03)00360-X

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：

Histone lysine methylation plays a key role in the organization of chromatin structure and the regulation of gene expression. Recent studies demonstrated that the yeast Set1 and Set2 histone methyltransferases are recruited to mRNA coding regions by the PAF transcription elongation complex in a manner dependent upon the phosphorylation state of the carboxy-terminal domain of RNA polymerase II. These studies define an unexpected link between transcription elongation and histone methylation.

引用

页码：429 / 432

页数：4

共 21 条

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