The PHD type zinc finger is an integral part of the CBP acetyltransferase domain.

  • Kalkhoven E
  • Teunissen H
  • Houweling A
 et al. 
  • 42

    Readers

    Mendeley users who have this article in their library.
  • 76

    Citations

    Citations of this article.

Abstract

Histone acetyltransferases (HATs) such as CBP and p300 are regarded as key regulators of RNA polymerase II-mediated transcription, but the critical structural features of their HAT modules remain ill defined. The HAT domains of CBP and p300 are characterized by the presence of a highly conserved putative plant homeodomain (PHD) (C4HC3) type zinc finger, which is part of the functionally uncharacterized cysteine-histidine-rich region 2 (CH2). Here we show that this region conforms to the PHD type zinc finger consensus and that it is essential for in vitro acetylation of core histones and the basal transcription factor TFIIE34 as well as for CBP autoacetylation. PHD finger mutations also reduced the transcriptional activity of the full-length CBP protein when tested on transfected reporter genes. Importantly, similar results were obtained on integrated reporters, which reflect a more natural chromatinized state. Taken together, our results indicate that the PHD finger forms an integral part of the enzymatic core of the HAT domain of CBP.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Eric Kalkhoven

  • Hans Teunissen

  • Ada Houweling

  • C Peter Verrijzer

  • Alt Zantema

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free