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    Mol Cell. 2004 Jan 30;13(2):265-77.

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

    Kukimoto I, Elderkin S, Grimaldi M, Oelgeschläger T, Varga-Weisz PD.

    Source

    Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, United Kingdom.

    Abstract

    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.

    PMID:
    14759371
    [PubMed - indexed for MEDLINE]

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