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A human RNA polymerase II complex containing factors that modify chromatin structure.

We have isolated a human RNA polymerase II complex that contains chromatin structure remodeling activity and histone acetyltransferase activity. This complex contains the Srb proteins, the Swi-Snf complex, and the histone acetyltransferases CBP and PCAF in addition to RNA polymerase II. Notably, the general transcription factors are absent from this complex. The complex was purified by two different methods: conventional chromatography and affinity chromatography using antibodies directed against CDK8, the human homolog of the yeast Srb10 protein. Protein interaction studies demonstrate a direct interaction between RNA polymerase II and the histone acetyltransferases p300 and PCAF. Importantly, p300 interacts specifically with the nonphosphorylated, initiation-competent form of RNA polymerase II. In contrast, PCAF interacts with the elongation-competent, phosphorylated form of RNA polymerase II.

Pubmed ID: 9710619


  • Cho H
  • Orphanides G
  • Sun X
  • Yang XJ
  • Ogryzko V
  • Lees E
  • Nakatani Y
  • Reinberg D


Molecular and cellular biology

Publication Data

September 10, 1998

Associated Grants

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

Mesh Terms

  • Acetyltransferases
  • Cell Cycle Proteins
  • Chromatin
  • Chromatography, Affinity
  • Chromatography, Gel
  • Cyclin-Dependent Kinase 8
  • Cyclin-Dependent Kinases
  • HeLa Cells
  • Histone Acetyltransferases
  • Humans
  • Phosphorylation
  • Protein-Serine-Threonine Kinases
  • RNA Polymerase II
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Transcription, Genetic
  • p300-CBP Transcription Factors