A new companion of elongating RNA Polymerase II: TINTIN, an independent sub-module of NuA4/TIP60 for nucleosome transactions

Transcription. 2014;5(5):e995571. doi: 10.1080/21541264.2014.995571. Epub 2015 Jan 7.


Multiple factors are involved in the elongation stage of transcription regulation to ensure the passing of RNA polymerases while preserving appropriate nucleosome structure thereafter. The recently reported trimeric sub-module of NuA4 histone acetyltransferase complex involved in this process provides more insight into the sophisticated modulation of transcription elongation.

Keywords: Eaf3; Eaf5; Eaf7; MRG15; MRGBP; NuA4; TINTIN; acetylation; chromatin; transcription elongation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Histone Acetyltransferases / metabolism
  • Humans
  • Lysine Acetyltransferase 5
  • Nucleosomes / metabolism*
  • RNA Polymerase II / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription Elongation, Genetic*
  • Transcription Factors / metabolism*


  • Nucleosomes
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Histone Acetyltransferases
  • KAT5 protein, human
  • Lysine Acetyltransferase 5
  • NuA4 protein, S cerevisiae
  • RNA Polymerase II