Abstract
Acetylation of lysine residues within the amino-terminal domains of the core histones plays a critical role in chromatin assembly as well as in regulation of gene expression. To study the biochemical function of histone acetylation, we have cloned a cDNA encoding the catalytic subunit of human histone acetyltransferase, Hat1. Analysis of the predicted amino acid sequence of human Hat1 revealed an open reading frame of 419 amino acids with a calculated molecular mass of 49.5 RDa and an isoelectric point of 5.5. The amino acid sequence of human Hat1 is homologous to those of known and putative Hat1 proteins from various species throughout the entire open reading frame. The recombinant human Hat1 protein expressed in bacteria possesses histone H4 acetyltransferase activity in vitro. Both RbAp46 and RbAp48, which participate in various processes of histone metabolism, enhance the histone acetyltransferase activity of the recombinant human Hat1, indicating that they are both able to functionally interact with the human Hat1 in vitro.
| Original language | English |
|---|---|
| Pages (from-to) | 484-491 |
| Number of pages | 8 |
| Journal | Journal of Biochemistry and Molecular Biology |
| Volume | 31 |
| Issue number | 5 |
| Publication status | Published - 1998 Sep 30 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
Cite this
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Cloning and characterization of the catalytic subunit of human histone acetyltransferase, Hat1. / Chung, Hyo Young; Suh, Na Young; Yoon, Jong Bok.
In: Journal of Biochemistry and Molecular Biology, Vol. 31, No. 5, 30.09.1998, p. 484-491.Research output: Contribution to journal › Article
TY - JOUR
T1 - Cloning and characterization of the catalytic subunit of human histone acetyltransferase, Hat1
AU - Chung, Hyo Young
AU - Suh, Na Young
AU - Yoon, Jong Bok
PY - 1998/9/30
Y1 - 1998/9/30
N2 - Acetylation of lysine residues within the amino-terminal domains of the core histones plays a critical role in chromatin assembly as well as in regulation of gene expression. To study the biochemical function of histone acetylation, we have cloned a cDNA encoding the catalytic subunit of human histone acetyltransferase, Hat1. Analysis of the predicted amino acid sequence of human Hat1 revealed an open reading frame of 419 amino acids with a calculated molecular mass of 49.5 RDa and an isoelectric point of 5.5. The amino acid sequence of human Hat1 is homologous to those of known and putative Hat1 proteins from various species throughout the entire open reading frame. The recombinant human Hat1 protein expressed in bacteria possesses histone H4 acetyltransferase activity in vitro. Both RbAp46 and RbAp48, which participate in various processes of histone metabolism, enhance the histone acetyltransferase activity of the recombinant human Hat1, indicating that they are both able to functionally interact with the human Hat1 in vitro.
AB - Acetylation of lysine residues within the amino-terminal domains of the core histones plays a critical role in chromatin assembly as well as in regulation of gene expression. To study the biochemical function of histone acetylation, we have cloned a cDNA encoding the catalytic subunit of human histone acetyltransferase, Hat1. Analysis of the predicted amino acid sequence of human Hat1 revealed an open reading frame of 419 amino acids with a calculated molecular mass of 49.5 RDa and an isoelectric point of 5.5. The amino acid sequence of human Hat1 is homologous to those of known and putative Hat1 proteins from various species throughout the entire open reading frame. The recombinant human Hat1 protein expressed in bacteria possesses histone H4 acetyltransferase activity in vitro. Both RbAp46 and RbAp48, which participate in various processes of histone metabolism, enhance the histone acetyltransferase activity of the recombinant human Hat1, indicating that they are both able to functionally interact with the human Hat1 in vitro.
UR - http://www.scopus.com/inward/record.url?scp=0032344823&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032344823&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0032344823
VL - 31
SP - 484
EP - 491
JO - BMB Reports
JF - BMB Reports
SN - 1976-6696
IS - 5
ER -