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

Susan McCracken, Nova Fong, Emanuel Rosonina, Krassimir Yankulov, Greg Brothers, David Siderovski, Andrew Hessel, Stephen Foster, Stewart Shuman, David L. Bentley

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435 Scopus citations

Abstract

We have investigated the role of the RNA Polymerase II (Pol II) carboxy- terminal domain (CTD) in mRNA 5'-capping. Transcripts made in vivo by Pol II with a truncated CTD had a lower proportion of capped 5' ends than those made by Pol II with a full-length CTD. In addition, the enzymes responsible for cap synthesis, RNA guanylyltransferase, and RNA (guanine-7)-methyltransferase bound directly to the phosphorylated, but not to the nonphosphorylated, form of the CTD in vitro. These results suggest that: (1) Pol II-specific capping of nascent transcripts in vivo is enhanced by recruitment of the capping enzymes to the CTD and (2) capping is co-ordinated with CTD phosphorylation.

Original languageEnglish
Pages (from-to)3306-3318
Number of pages13
JournalGenes and Development
Volume11
Issue number24
DOIs
StatePublished - 15 Dec 1997

Keywords

  • CTD
  • MRNA cap
  • RNA 7-methyltransferase
  • RNA Pol II
  • RNA guanylyltransferase

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