HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins.
Chromatin remodelling complexes containing the nucleosome-dependent ATPase ISWI were first isolated from Drosophila embryos (NURF, CHRAC and ACF). ISWI was the only common component reported in these complexes. Our purification of human CHRAC (HuCHRAC) shows that ISWI chromatin remodelling complexes can have a conserved subunit composition in completely different cell ... types, suggesting a conserved function of ISWI. We show that the human homologues of two novel putative histone-fold proteins in Drosophila CHRAC are present in HuCHRAC. The two human histone-fold proteins form a stable complex that binds naked DNA but not nucleosomes. HuCHRAC also contains human ACF1 (hACF1), the homologue of Acf1, a subunit of Drosophila ACF. The N-terminus of mouse ACF1 was reported as a heterochromatin-targeting domain. hACF1 is a member of a family of proteins with a related domain structure that all may target heterochromatin. We discuss a possible function for HuCHRAC in heterochromatin dynamics. HuCHRAC does not contain topoisomerase II, which was reported earlier as a subunit of Drosophila CHRAC.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Animals, DNA Polymerase III, DNA-Binding Proteins, Drosophila, Drosophila Proteins, Hela Cells, Histones, Humans, Mice, Molecular Sequence Data, Nucleoproteins, Nucleosomes, Protein Binding, Protein Folding, Recombinant Proteins, Sequence Homology, Amino Acid, Transcription Factors
Adenosine Triphosphatases, Amino Acid Sequence, Animals, DNA Polymerase III, DNA-Binding Proteins, Drosophila, Drosophila Proteins, Hela Cells, Histones, Humans, Mice, Molecular Sequence Data, Nucleoproteins, Nucleosomes, Protein Binding, Protein Folding, Recombinant Proteins, Sequence Homology, Amino Acid, Transcription Factors
EMBO J.
Date: Jul. 03, 2000
PubMed ID: 10880450
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