Abstract:
:Much controversy exists regarding the structural organization of the yeast centromeric nucleosome and the role of the nonhistone protein, Scm3, in its assembly and architecture. Here we show that the substitution of H3 with its centromeric variant Cse4 results in octameric nucleosomes that organize DNA in a left-handed superhelix. We demonstrate by single-molecule approaches, micrococcal nuclease digestion and small-angle X-ray scattering that Cse4-nucleosomes exhibit an open conformation with weakly bound terminal DNA segments. The Cse4-octamer does not preferentially form nucleosomes on its cognate centromeric DNA. We show that Scm3 functions as a Cse4-specific nucleosome assembly factor, and that the resulting octameric nucleosomes do not contain Scm3 as a stably bound component. Taken together, our data provide insights into the assembly and structural features of the budding yeast centromeric nucleosome.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Dechassa ML,Wyns K,Li M,Hall MA,Wang MD,Luger Kdoi
10.1038/ncomms1320subject
Has Abstractpub_date
2011-01-01 00:00:00pages
313issn
2041-1723pii
ncomms1320journal_volume
2pub_type
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