Howe L, Ausió J
Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
Mol Cell Biol. 1998 Mar;18(3):1156-62. doi: 10.1128/MCB.18.3.1156.
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.
我们试图研究组蛋白八聚体对九锌指蛋白转录因子IIIA(TFIIIA)施加的结合限制。为此,将非洲爪蟾卵母细胞和体细胞5S rRNA基因的五个重叠片段重构成核小体,随后发现核小体平移定位是TFIIIA与5S rRNA基因结合的主要决定因素。此外,还发现组蛋白乙酰化不能克服不利平移位置所施加的TFIIIA结合限制。