Abstract
Tip60, originally isolated as an HIV-1-Tat interactive protein, contains an evolutionarily conserved domain with yeast silencing factors. We demonstrate here direct biochemical evidence that this domain of Tip60 has histone acetyltransferase activity. The purified recombinant effectively acetylates H2A, H3, and H4 but not H2B of core histone mixtures. This substrate specificity has not been observed among histone acetyltransferases analyzed to date. These results indicate that Tip60 is a histone acetyltransferase with a novel property, suggesting that Tip60 and its related factors may introduce a distinct alteration on chromatin.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acetyltransferases / metabolism*
-
Amino Acid Sequence
-
Cell Nucleus / metabolism
-
Histone Acetyltransferases
-
Humans
-
Lysine Acetyltransferase 5
-
Molecular Sequence Data
-
Peptide Fragments / chemistry
-
Peptide Fragments / metabolism
-
Proteins / genetics
-
Proteins / metabolism*
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / metabolism
-
Saccharomyces cerevisiae / metabolism
-
Saccharomyces cerevisiae Proteins*
-
Substrate Specificity
Substances
-
Peptide Fragments
-
Proteins
-
Recombinant Proteins
-
Saccharomyces cerevisiae Proteins
-
Acetyltransferases
-
Histone Acetyltransferases
-
KAT5 protein, human
-
Lysine Acetyltransferase 5