# Molecular cloning, expression and functional interaction of p48 subunit of chicken chromatin assembly factor 1 with histone deacetylase 2 and histone acetyltransferase 1
> Ahmad A.

URL kanonis: https://discover.unhas.ac.id/publications/pub_scopus_84986005653
Jurnal / Konferensi: Indonesian Journal of Chemistry
Tahun terbit: 2012
DOI: https://doi.org/10.22146/ijc.21375
ISSN: 14119420
Kuartil SJR: Q3
Citations: 0

## Authors
- Ahmad A.

## Abstract
We cloned and sequenced cDNA encoding p48 subunit of the chicken CAF-1, chCAF-1p48, and histone acetyltransferase-1, chHAT-1 from chicken DT40 cell lines. We showed that the p48 subunit of CAF-1 tightly binds to two regions of chicken histone deacetylase 2, chHDAC-2, located between amino acid residues 82-180 and 245-314, respectively. We also established that two N-terminal, two C-terminal, or one N-terminal and one C-terminal WD repeat motif of chCAF-1p48 are required for this interaction. The GST pulldown assay, involving truncated and missense mutants of chCAF-1p48, revealed not only that a region containing the seventh WD dipeptide motif of chCAF-1p48, comprising amino acids 376-405, binds to chHAT-1 in vitro, but also that mutation of the motif has no influence on the in vitro interaction. We also established that the region, which is located between amino acids 380-408 of chHAT-1 and contains a leucine zipper motif, is required for its in vitro interaction with chCAF-1p48. Mutation on each of four Leu residues in the leucine zipper motif of chHAT-1 causes the disappearance of the interaction with chCAF-1p48. These results should be useful information for understanding the participation of chCAF-1p48 protein as histones chaperone in DNA-utilizing processes, such as replication, recombination, repair and gene expression in DT40 chicken B cell.

## Keywords
- Leucine zipper
- Chemistry
- Molecular biology
- Histone acetyltransferase
- bZIP domain
- Histone deacetylase
- Histone
- Biochemistry
- Gene
- Peptide sequence
- Biology

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Sumber: Discover Unhas — RIMS Universitas Hasanuddin.
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