Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A

Nature. 1998 Nov 12;396(6707):184-6. doi: 10.1038/24190.


Transforming viral proteins such as E1A force cells through the restriction point of the cell cycle into S phase by forming complexes with two cellular proteins: the retinoblastoma protein (Rb), a transcriptional co-repressor, and CBP/p300, a transcriptional co-activator. These two proteins locally influence chromatin structure: Rb recruits a histone deacetylase, whereas CBP is a histone acetyltransferase. Progression through the restriction point is triggered by phosphorylation of Rb, leading to disruption of Rb-associated repressive complexes and allowing the activation of S-phase genes. Here we show that CBP, like Rb, is controlled by phosphorylation at the G1/S boundary, increasing its histone acetyltransferase activity. This enzymatic activation is mimicked by E1A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Acetyltransferases / metabolism*
  • Adenovirus E1A Proteins / metabolism*
  • Animals
  • CDC2-CDC28 Kinases*
  • CREB-Binding Protein
  • Cell Cycle*
  • Cyclin E / metabolism*
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases / metabolism*
  • Enzyme Activation
  • G1 Phase
  • Histone Acetyltransferases
  • Mice
  • Nuclear Proteins / metabolism*
  • Oncogene Proteins / metabolism*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • S Phase
  • Saccharomyces cerevisiae Proteins*
  • Trans-Activators / metabolism*
  • Transcriptional Activation
  • Transfection


  • Adenovirus E1A Proteins
  • Cyclin E
  • Nuclear Proteins
  • Oncogene Proteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Acetyltransferases
  • CREB-Binding Protein
  • Crebbp protein, mouse
  • Histone Acetyltransferases
  • Protein Serine-Threonine Kinases
  • CDC2-CDC28 Kinases
  • Cdk2 protein, mouse
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases