Interaction of RNA polymerase II with acetylated nucleosomal core particles.
Chemical acetylation of nucleosomal cores is accompanied by an increase in their efficiency as in vitro transcription templates. Low amounts of acetic anhydride cause preferential modification of the amino-terminal tails of core histones. Modification of these domains, which causes moderate structural effects, is apparently correlated with the observed stimulation of RNA synthesis. In contrast, extensive modification of the globular regions of core histones, which is accompanied by a large structural relaxation of the particle, causes little additional effect on transcription. Acetylation of the amino-terminal domains of histones might stimulate transcription by changing the interaction of the histone tails with components of the transcriptional machinery.
Piñeiro
M
M
Centro de Biología Molecular, Universidad Autónoma de Madrid, Spain.
González
P J
PJ
Hernández
F
F
Palacián
E
E
D000089:Acetic Anhydrides / Q000494:pharmacology; D000107:Acetylation; D000818:Animals; D002645:Chickens; D003570:Cytidine Triphosphate / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D007700:Kinetics; D009707:Nucleosomes / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D012313:RNA / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D012319:RNA Polymerase II / Q000378:metabolism*; D014158:Transcription, Genetic; D014544:Uridine Triphosphate / Q000378:metabolism
D000089:Acetic Anhydrides; D006657:Histones; D009707:Nucleosomes; D010761:Phosphorus Radioisotopes; C031800:acetic anhydride; D012313:RNA; D003570:Cytidine Triphosphate; D012319:RNA Polymerase II; D014544:Uridine Triphosphate