A Novel Histone Acetyltransferase Is an Integral Subunit of Elongating RNA Polymerase II Holoenzyme

Mol Cell. 1999 Jul;4(1):123-8. doi: 10.1016/s1097-2765(00)80194-x.

Abstract

The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a role for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetyltransferases / chemistry
  • Acetyltransferases / genetics*
  • Amino Acid Sequence
  • Chromatin / chemistry
  • Cloning, Molecular
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Gene Deletion
  • Histone Acetyltransferases
  • Molecular Sequence Data
  • Phenotype
  • RNA Polymerase II / chemistry
  • RNA Polymerase II / metabolism*
  • Recombinant Proteins / genetics
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment

Substances

  • Chromatin
  • Fungal Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases
  • RNA Polymerase II

Associated data

  • GENBANK/AB012248
  • GENBANK/AC004373
  • GENBANK/O14023
  • GENBANK/Q02908
  • GENBANK/Q23651