Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding - PubMed (original) (raw)

. 2005 Jan 21;280(3):1817-25.

doi: 10.1074/jbc.M411347200. Epub 2004 Oct 30.

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Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding

Young-Jun Park et al. J Biol Chem. 2005.

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Abstract

Eukaryotic chromatin is highly dynamic and turns over rapidly even in the absence of DNA replication. Here we show that the acidic histone chaperone nucleosome assembly protein 1 (NAP-1) from yeast reversibly removes and replaces histone protein dimer H2A-H2B or histone variant dimers from assembled nucleosomes, resulting in active histone exchange. Transient removal of H2A-H2B dimers facilitates nucleosome sliding along the DNA to a thermodynamically favorable position. Histone exchange as well as nucleosome sliding is independent of ATP and relies on the presence of the C-terminal acidic domain of yeast NAP-1, even though this region is not required for histone binding and chromatin assembly. Our results suggest a novel role for NAP-1 (and perhaps other acidic histone chaperones) in mediating chromatin fluidity by incorporating histone variants and assisting nucleosome sliding. NAP-1 may function either untargeted (if acting alone) or may be targeted to specific regions within the genome through interactions with additional factors.

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