Data from: Cryo-electron tomography reveals the multiplex anatomy of condensed native chromatin and its unfolding by histone citrullination
Nucleosome chains fold and self-associate to form higher order structures whose internal organization is unknown. Here, cryo-electron tomography (cryo-ET) of native human chromatin reveals novel folding motifs such as 1) non-uniform nucleosome stacking, 2) intermittent parallel and perpendicular ori...
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Zusammenfassung: | Nucleosome chains fold and self-associate to form higher order structures
whose internal organization is unknown. Here, cryo-electron tomography
(cryo-ET) of native human chromatin reveals novel folding motifs such as
1) non-uniform nucleosome stacking, 2) intermittent parallel and
perpendicular orientations of adjacent nucleosome planes, and 3) an
inverse zigzag nucleosome chain path, which deviates from the direct
zigzag topology seen in reconstituted nucleosomal arrays. By examining
these self-associated structures, we observed prominent nucleosome
stacking in-cis and anti-parallel nucleosome interactions in-trans, which
are consistent with partial nucleosome interdigitation. Histone
citrullination strongly inhibits nucleosome stacking and self-association
with a modest effect on chromatin folding, while the reconstituted arrays
showed a zigzag topology which undergoes a dramatic unfolding induced by
histone citrullination. This study sheds light on the internal structure
of compact chromatin nanoparticles and suggests a novel mechanism for how
epigenetic changes in chromatin are retained across both open and
condensed forms of chromatin. |
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DOI: | 10.5061/dryad.ttdz08m21 |