Howe L, Itoh T, Katagiri C, Ausio J
Department of Biochemistry and Microbiology, University of Victoria, B.C., Canada.
Biochemistry. 1998 Feb 3;37(5):1174-7. doi: 10.1021/bi972723+.
In an attempt to understand the mechanism by which transcription factors compete with histone octamers for cognate binding sites in chromatin, the effect of the histone binding protein nucleoplasmin on the binding of TFIIIA to nucleosomal 5S rRNA genes was tested. In this study, it was shown that, despite the previously reported nucleosome remodeling ability of nucleoplasmin, the binding of TFIIIA to nucleosomal DNA cannot be facilitated by this protein. Furthermore, it was demonstrated that nucleoplasmin cannot overcome nucleosome mediated repression of transcription of reconstituted 5S rRNA genes. In contrast to earlier work, this study used a homologous system composed of the 5S rRNA gene, nucleoplasmin, and TFIIIA from Xenopus laevis.
为了理解转录因子与组蛋白八聚体在染色质中竞争同源结合位点的机制,研究了组蛋白结合蛋白核质素对TFIIIA与核小体5S rRNA基因结合的影响。在本研究中,结果表明,尽管先前报道核质素有核小体重塑能力,但该蛋白并不能促进TFIIIA与核小体DNA的结合。此外,还证明核质素无法克服核小体介导的重组5S rRNA基因转录抑制。与早期工作不同,本研究使用了由非洲爪蟾的5S rRNA基因、核质素和TFIIIA组成的同源系统。