Nucleosome translational position, not histone acetylation, determines TFIIIA binding to nucleosomal Xenopus laevis 5S rRNA genes.
We sought to study the binding constraints placed on the nine-zinc-finger protein transcription factor IIIA (TFIIIA) by a histone octamer. To this end, five overlapping fragments of the Xenopus laevis oocyte and somatic 5S rRNA genes were reconstituted into nucleosomes, and it was subsequently shown that nucleosome translational positioning is a major determinant of the binding of TFIIIA to the 5S rRNA genes. Furthermore, it was found that histone acetylation cannot override the TFIIIA binding constraints imposed by unfavorable translational positions.
Howe
L
L
Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
Ausió
J
J
D000107:Acetylation; D000818:Animals; D001665:Binding Sites; D018983:DNA Footprinting; D004268:DNA-Binding Proteins / Q000378:metabolism*; D003850:Deoxyribonuclease I / Q000378:metabolism; D006367:HeLa Cells; D006657:Histones / Q000235:genetics*; D006801:Humans; D009707:Nucleosomes / Q000378:metabolism*; D009865:Oocytes; D014176:Protein Biosynthesis; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic; D014982:Xenopus laevis / Q000235:genetics*; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D006657:Histones; D009707:Nucleosomes; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D003850:Deoxyribonuclease I