Transcriptional properties of oligonucleosomal templates containing acetylated (H3-H4)2 tetramers.
Direct chemical acetylation of an oligonucleosomal template for bacteriophage T7 RNA polymerase is accompanied by a substantial increase in its capability to support RNA synthesis. The template was assembled from a plasmid, containing a promoter and a terminator for T7 RNA polymerase, plus one (H3-H4)2 tetramer and two H2A.H2B dimers for each 200 base pairs of DNA. Under the employed conditions, acetylation modifies in a preferential way the lysine residues located in the amino-terminal domains of core histones. When the template is assembled with acetylated tetramers and untreated dimers, its efficiency in promoting RNA synthesis is also largely increased. Since a previous work reported transcriptional stimulation upon acetylation of H2A.H2B dimers [Puerta et al. (1995) Biochem. Biophys. Res. Commun. 210, 409], the transcriptional repression brought about by core histone octamers seems to require that the amino-terminal domains of both (H3.H4)2 tetramers and H2A.H2B dimers are not acetylated.
Hernández
F
F
Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones, Científicas, Cantoblanco, Madrid, Spain.
Puerta
C
C
López-Alarcón
L
L
Palacián
E
E
D000107:Acetylation; D017123:Bacteriophage T7 / Q000201:enzymology; D002850:Chromatography, Gel; D003570:Cytidine Triphosphate / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008239:Lysine; D046911:Macromolecular Substances; D009707:Nucleosomes / Q000378:metabolism*; D010957:Plasmids; D013698:Templates, Genetic; D014158:Transcription, Genetic; D014764:Viral Proteins
D006657:Histones; D046911:Macromolecular Substances; D009707:Nucleosomes; D014764:Viral Proteins; D003570:Cytidine Triphosphate; C062210:bacteriophage T7 RNA polymerase; D012321:DNA-Directed RNA Polymerases; D008239:Lysine