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Papers In Press, published online ahead of print December 17, 2001
Department of Medicine, University of Washington, Seattle, WA 98195-7720
Corresponding Author: gstam{at}u.washington.edu
The Sp1/KLF family of factors regulates diverse cellular processes including growth and development. FKLF2 is a new member of this family. In this study, we characterized the coactivators involved in FKLF2 transcriptional activation. Our results show that both CBP/p300 and PCAF enhance FKLF2 transcriptional activity. We demonstrate that the acetyltransferase activity of PCAF but not that of CBP/p300 is required for stimulating FKLF2 transcription activity. We further show that p300 and PCAF act cooperatively in stimulating FKLF2 transcriptional activation. FKLF2 interacts with both CBP and PCAF through specific domains, and CBP and PCAF acetylate FKLF2. Both CBP/p300 and PCAF stimulate FKLF2 DNA binding activity. The integrity of the acetyltransferase domain of PCAF but not that of CBP/p300 is required for stimulating FKLF2 DNA binding activity. These results demonstrate that CBP/p300 and PCAF stimulate FKLF2 transcriptional activity at least by enhancing its DNA binding. The acetyltransferase activity of CBP/p300 and PCAF play distinct role in stimulating FKLF2 transcription and DNA binding.
J. Biol. Chem, 10.1074/jbc.M108826200
Submitted on September 13, 2001
Revised on December 7, 2001
Accepted on December 17, 2001
Functional interaction between coactivators CBP/p300, PCAF and transcription factor FKLF2
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