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Human Elongator facilitates RNA polymerase II transcription through chromatin.

A human Elongator complex was purified from HeLa cells and found to be composed of three polypeptides. Human Elongator contains histone acetyltransferase activity with specificity to histone H3 and, to a much lesser extent, to histone H4. Although many reports have suggested a role for the yeast Elongator in transcription elongation through chromatin templates, no direct evidence supporting this function exists. In the present study, we demonstrate that the human Elongator facilitates transcription by RNA polymerase II in a chromatin- and acetyl-CoA-dependent manner. The complex was found to directly interact with RNA polymerase II but failed to interact with other factors that facilitated RNA polymerase II to traverse through nucleosomes. From our results, we postulate that different mechanisms operate to ensure efficient transcription by RNA polymerase II on chromatin templates.

Pubmed ID: 11818576


  • Kim JH
  • Lane WS
  • Reinberg D


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

February 5, 2002

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM-37120

Mesh Terms

  • Acetyl Coenzyme A
  • Acetyltransferases
  • Amino Acid Sequence
  • Binding Sites
  • Chromatin
  • Gene Expression Regulation
  • HeLa Cells
  • Histone Acetyltransferases
  • Histones
  • Humans
  • Molecular Sequence Data
  • Protein Subunits
  • RNA Polymerase II
  • Saccharomyces cerevisiae Proteins
  • Substrate Specificity
  • Templates, Genetic
  • Transcription, Genetic