The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF.

The histone fold is a structural motif with which two related proteins interact and is found in complexes involved in wrapping DNA, the nucleosome, and transcriptional regulation, as in NC2. We reveal a novel function for histone-fold proteins: facilitation of nucleosome remodeling. ACF1-ISWI complex (ATP-dependent chromatin assembly and remodeling factor ...
[ACF]) associates with histone-fold proteins (CHRAC-15 and CHRAC-17 in the human chromatin accessibility complex [CHRAC]) whose functional relevance has been unclear. We show that these histone-fold proteins facilitate ATP-dependent nucleosome sliding by ACF. Direct interaction of the CHRAC-15/17 complex with the ACF1 subunit is essential for this process. CHRAC-17 interacts with another histone-fold protein, p12, in DNA polymerase epsilon, but CHRAC-15 is essential for interaction with ACF and enhancement of nucleosome sliding. Surprisingly, CHRAC-15/17, p12/CHRAC-17, and NC2 complexes facilitate ACF-mediated chromatin assembly by a mechanism different from nucleosome sliding enhancement, suggesting a general activity of H2A/H2B type histone-fold complexes in chromatin assembly.
Mesh Terms:
Amino Acid Sequence, Animals, Chromatin, DNA, DNA Polymerase II, DNA Polymerase III, DNA-Binding Proteins, Dose-Response Relationship, Drug, Drosophila, Glutathione Transferase, Histones, Humans, Molecular Sequence Data, Nucleoproteins, Nucleosomes, Protein Binding, Protein Folding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Time Factors
Mol. Cell
Date: Jan. 30, 2004
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