Nucleic Acids Research, Vol 26, Issue 12 2948-2954, Copyright © 1998 by Oxford University Press
ER Smith, JM Belote, RL Schiltz, XJ Yang, PA Moore, SL Berger, Y Nakatani and CD Allis
PCAF and hGCN5 are distinct human genes that encode proteins related to the
yeast histone acetyltransferase and transcriptional adapter GCN5. The PCAF
protein shares extensive similarity with the 439 amino acids of yGCN5, but
it has an approximately 350 amino acid N-terminal extension that interacts
with the transcriptional co-activator p300/CBP. Adenoviral protein E1a can
disrupt PCAF-CBP interactions and prevent PCAF-dependent cellular
differentiation. In this report, we describe the cloning and initial
characterization of a Drosophila homolog of yGCN5. In addition to the
homology to yGCN5, the Drosophila protein shares sequencesimilarity with
the N-terminal portion of human PCAF that is involved in binding to CBP. In
the course of characterizing dGCN5, we have discovered that hGCN5 also
contains an N- terminal extension with significant similarity to PCAF.
Interestingly, in the case of the h GCN5 gene, alternative splicing may
regulate the production of full-length hGCN5. The presence of the
N-terminal domain in a Drosophila GCN5 homolog and both human homologs
suggests that it was part of the ancestral form of metazoan GCN5.
ARTICLES
Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members
Department of Biology, University of Rochester, Rochester, NY 14627, USA.
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