The Length, Phosphorylation State, and Primary Structure of the RNA Polymerase II Carboxyl-terminal Domain Dictate Interactions with mRNA Capping Enzymes-Reference-Cited by-同舟云学术

The Length, Phosphorylation State, and Primary Structure of the RNA Polymerase II Carboxyl-terminal Domain Dictate Interactions with mRNA Capping Enzymes

Published:2001-07 Issue:30 Volume:276 Page:28075-28082
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pei Yi,Hausmann Stéphane,Ho C. Kiong,Schwer Beate,Shuman Stewart

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. Structure, mechanism, and evolution of the mRNA capping apparatus

2. 5′-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II

3. The Guanylyltransferase Domain of Mammalian mRNA Capping Enzyme Binds to the Phosphorylated Carboxyl-terminal Domain of RNA Polymerase II

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

5. Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II

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