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.
Kukimoto
Iwao
I
Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, United Kingdom.
Elderkin
Sarah
S
Grimaldi
Margaret
M
Oelgeschläger
Thomas
T
Varga-Weisz
Patrick D
PD
D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000737:chemistry; D004247:DNA / Q000737:chemistry; D004257:DNA Polymerase II / Q000737:chemistry; D004258:DNA Polymerase III / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry; D004305:Dose-Response Relationship, Drug; D004330:Drosophila; D005982:Glutathione Transferase / Q000378:metabolism; D006657:Histones / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D009698:Nucleoproteins / Q000737:chemistry; D009707:Nucleosomes / Q000737:chemistry*; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013997:Time Factors
C413904:CHRAC1 protein, human; D002843:Chromatin; D004268:DNA-Binding Proteins; D006657:Histones; D009698:Nucleoproteins; D009707:Nucleosomes; C413905:POLE3 protein, human; D011993:Recombinant Fusion Proteins; D004247:DNA; D005982:Glutathione Transferase; D004257:DNA Polymerase II; D004258:DNA Polymerase III