Transcriptional inhibitory role of the tail domains of histone (H3 x H4)2 tetramers.
Histone-DNA templates for bacteriophage T7 RNA polymerase were assembled from a plasmid containing a promoter and a terminator for this polymerase, (H3 x H4)2 tetramers deprived of their tail domains, and H2A x H2B dimers. Histone (H3 x H4)2 tetramers lacking their terminal domains were obtained from trypsin-digested nucleosomal cores. The oligonucleosomal templates containing (H3 x H4)2 tetramers lacking their tail domains, like the control templates with intact core histone octamers, protect approximately 146 base pairs of DNA against micrococcal nuclease digestion. The transcriptional inhibition caused by the association of DNA with core histone octamers is significantly reduced upon elimination of the tail domains of the (H3 x H4)2 tetramers. Apparently, the terminal domains of (H3 x H4)2 must be present to block transcription efficiently. These results show the important inhibitory role played by the tail domains of the histone (H3 x H4)2 tetramers, suggesting the involvement of these regions in transcriptional regulation.
Hernández
F
F
Consejo Superior de Investigaciones, Científicas and Universidad Autónoma de Madrid, Cantoblanco, Madrid, 28049, Spain.
López-Alarcón
L
L
Puerta
C
C
Palacián
E
E
D000818:Animals; D017123:Bacteriophage T7 / Q000235:genetics; D002645:Chickens; D012321:DNA-Directed RNA Polymerases / Q000235:genetics; D019281:Dimerization; D006657:Histones / Q000235:genetics / Q000502:physiology*; D009707:Nucleosomes / Q000235:genetics; D010446:Peptide Fragments / Q000502:physiology*; D011485:Protein Binding; D013698:Templates, Genetic; D014158:Transcription, Genetic / Q000187:drug effects
D006657:Histones; D009707:Nucleosomes; D010446:Peptide Fragments; D012321:DNA-Directed RNA Polymerases