Characterization of transcriptional regulatory domains of ankyrin repeat cofactor-1

Biochem Biophys Res Commun. 2007 Jul 13;358(4):1034-40. doi: 10.1016/j.bbrc.2007.05.017. Epub 2007 May 11.


The ankyrin repeats cofactor-1 (ANCO-1) was recently identified as a p160 coactivator-interacting protein that may inhibit transcriptional activity of nuclear receptors. Here, we have characterized the transcriptional regulatory domains of ANCO-1. Two intrinsic repression domains (RD) were identified: an N-terminal RD1 at residues 318-611 and a C-terminal RD2 at 2369-2663. ANCO-1 also contains an activation domain (AD) capable of stimulating transcription in both mammalian and yeast cells. The minimal AD was delimited to a 70-amino acid region at residues 2076-2145. Overall, full-length ANCO-1 exhibited transcriptional repressor activity, suggesting that RD domains may suppress the AD activity. We further demonstrated that ANCO-1 silencing by siRNA enhanced progesterone receptor-mediated transcription. Together, these results indicate that the transcriptional potential of ANCO-1 may be modulated by a combination of repression and activation signals.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • COS Cells
  • Chlorocebus aethiops
  • HeLa Cells
  • Humans
  • Promoter Regions, Genetic / genetics*
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Cytoplasmic and Nuclear / genetics*
  • Regulatory Elements, Transcriptional / genetics*
  • Repressor Proteins / chemistry*
  • Transcription Factors / genetics*
  • Transcription, Genetic / genetics*
  • Transcriptional Activation / genetics*


  • ANKRD11 protein, human
  • Receptors, Cytoplasmic and Nuclear
  • Repressor Proteins
  • Transcription Factors