The chromatin remodeller ACF acts as a dimeric motor to space nucleosomes

Lisa R. Racki, Janet G. Yang, Nariman Naber, Peretz D. Partensky, Ashley Acevedo, Thomas J. Purcell, Roger Cooke, Yifan Cheng () and Geeta J. Narlikar ()
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Lisa R. Racki: University of California, 600 16th Street
Janet G. Yang: University of California, 600 16th Street
Nariman Naber: University of California, 600 16th Street
Peretz D. Partensky: University of California, 600 16th Street
Ashley Acevedo: University of California, 600 16th Street
Thomas J. Purcell: University of California, 600 16th Street
Yifan Cheng: University of California, 600 16th Street
Geeta J. Narlikar: University of California, 600 16th Street

Nature, 2009, vol. 462, issue 7276, 1016-1021

Abstract: Abstract Evenly spaced nucleosomes directly correlate with condensed chromatin and gene silencing. The ATP-dependent chromatin assembly factor (ACF) forms such structures in vitro and is required for silencing in vivo. ACF generates and maintains nucleosome spacing by constantly moving a nucleosome towards the longer flanking DNA faster than the shorter flanking DNA. How the enzyme rapidly moves back and forth between both sides of a nucleosome to accomplish bidirectional movement is unknown. Here we show that nucleosome movement depends cooperatively on two ACF molecules, indicating that ACF functions as a dimer of ATPases. Further, the nucleotide state determines whether the dimer closely engages one or both sides of the nucleosome. Three-dimensional reconstruction by single-particle electron microscopy of the ATPase–nucleosome complex in an activated ATP state reveals a dimer architecture in which the two ATPases face each other. Our results indicate a model in which the two ATPases work in a coordinated manner, taking turns to engage either side of a nucleosome, thereby allowing processive bidirectional movement. This novel dimeric motor mechanism differs from that of dimeric motors such as kinesin and dimeric helicases that processively translocate unidirectionally and reflects the unique challenges faced by motors that move nucleosomes.

Date: 2009
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DOI: 10.1038/nature08621

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