Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Hernández F,Puerta C,López-Alarcón L,Palacián Edoi
10.1006/bbrc.1995.2121subject
Has Abstractpub_date
1995-08-04 00:00:00pages
232-8issue
1eissn
0006-291Xissn
1090-2104pii
S0006291X85721213journal_volume
213pub_type
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