Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain

被引：86

作者：

Cho, EJ ^{[1
]}

Rodriguez, CR ^{[1
]}

Takagi, T ^{[1
]}

Buratowski, S ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Boston, MA 02115 USA

来源：

GENES & DEVELOPMENT | 1998年 / 12卷 / 22期

关键词：

D O I：

10.1101/gad.12.22.3482

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

mRNA capping is a cotranscriptional event mediated by the association of capping enzyme with the phosphorylated carboxy-terminal domain (CTD) of RNA polymerase II. In the yeast Saccharomyces cerevisiae, capping enzyme is composed of two subunits, the mRNA 5'-triphosphatase (Cet1) and the mRNA guanylyltransferase (Ceg1). Here we map interactions between Ceg1, Cet1, and the CTD. Although the guanylyltransferase subunit can bind alone to the CTD, it cannot be guanylylated unless the triphosphatase subunit is also present. Therefore, the yeast mRNA guanylyltransferase is regulated by allosteric interactions with both the triphosphatase and CTD.

引用

页码：3482 / 3487

页数：6

共 24 条

[1] mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain [J].