A positive role for histone acetylation in transcription factor access to nucleosomal DNA

DY Lee, JJ Hayes, D Pruss, AP Wolffe - Cell, 1993 - cell.com
DY Lee, JJ Hayes, D Pruss, AP Wolffe
Cell, 1993cell.com
Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by
TFlllA of the 5s RNA gene wlthin model chromatin templates. This effect is independent of a
reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is
also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal
of the N-terminal tails from the core histones alsofacilitates the association of TFIIIA with
nucleosomal templates. We suggest that the histone tails have a major role in restrkting …
Summary
Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by TFlllA of the 5s RNA gene wlthin model chromatin templates. This effect is independent of a reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal of the N-terminal tails from the core histones alsofacilitates the association of TFIIIA with nucleosomal templates. We suggest that the histone tails have a major role in restrkting transcriptfon factor access to DNA and that their acetylation releases this restriction by directing dissociation of the tails from DNA and/or inducing a change in DNA configuration on the histone core to allow transcription factor binding. Acetylation of core histones might be expected to exert a major influence on the accessibility of chromatin to regulatory molecules.
cell.com