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Single‐molecule nucleosome remodeling by INO 80 and effects of histone tails
Author(s) -
Schwarz Marianne,
Schall Kevin,
Kallis Eleni,
Eustermann Sebastian,
Guariento Mara,
Moldt Manuela,
Hopfner KarlPeter,
Michaelis Jens
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12973
Subject(s) - nucleosome , chromatin , chromatin remodeling , histone , swi/snf , chromatosome , microbiology and biotechnology , biophysics , förster resonance energy transfer , biology , chemistry , histone code , genetics , dna , physics , quantum mechanics , fluorescence
Genome maintenance and integrity requires continuous alterations of the compaction state of the chromatin structure. Chromatin remodelers, among others the INO 80 complex, help organize chromatin by repositioning, reshaping, or evicting nucleosomes. We report on INO 80 nucleosome remodeling, assayed by single‐molecule Foerster resonance energy transfer on canonical nucleosomes as well as nucleosomes assembled from tailless histones. Nucleosome repositioning by INO 80 is a processively catalyzed reaction. During the initiation of remodeling, probed by the INO 80 bound state, the nucleosome reveals structurally heterogeneous states for tailless nucleosomes (in contrast to wild‐type nucleosomes). We, therefore, propose an altered energy landscape for the INO 80‐mediated nucleosome sliding reaction in the absence of histone tails.