Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding. Journal Article uri icon

Overview

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.

publication date

  • January 21, 2005

Full Author List

  • Park Y-J; Chodaparambil JV; Bao Y; McBryant SJ; Luger K

Other Profiles

Additional Document Info

start page

  • 1817

end page

  • 1825

volume

  • 280

issue

  • 3