Elongator interactions with nascent mRNA revealed by RNA immunoprecipitation

Mol Cell. 2004 May 21;14(4):457-64. doi: 10.1016/s1097-2765(04)00239-4.

Abstract

The histone acetyltransferase Elongator was originally isolated as a component of the elongating form of RNA polymerase II (RNAPII) and a plethora of data has since supported a role for the factor in transcription. However, recent data has suggested that it is predominantly cytoplasmic and does not associate with the DNA of transcribed genes in vivo. Here, we report that Elongator binds to RNA both in vitro and in vivo. Using a modified chromatin immunoprecipitation procedure, RNA immunoprecipitation (RIP), we show that Elongator is indeed present at several actively transcribed genes and that it associates with the nascent RNA emanating from elongating RNAPII along the entire coding region of a gene. These results strongly support a role for Elongator in transcript elongation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism*
  • Binding Sites / genetics
  • Genes, Regulator / genetics*
  • Histone Acetyltransferases
  • Macromolecular Substances
  • Precipitin Tests / methods
  • Protein Binding / genetics
  • RNA Cap-Binding Proteins / genetics
  • RNA Cap-Binding Proteins / metabolism
  • RNA Polymerase I / genetics
  • RNA Polymerase I / metabolism
  • RNA Polymerase II / genetics
  • RNA Polymerase II / metabolism*
  • RNA, Messenger / biosynthesis*
  • RNA, Messenger / genetics
  • RNA, Ribosomal / genetics
  • RNA, Ribosomal / metabolism
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Transcription, Genetic / genetics

Substances

  • Macromolecular Substances
  • RNA Cap-Binding Proteins
  • RNA, Messenger
  • RNA, Ribosomal
  • Acetyltransferases
  • Histone Acetyltransferases
  • RNA Polymerase II
  • RNA Polymerase I