期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1983
卷号：80
期号：8
页码：2142-2145
DOI：10.1073/pnas.80.8.2142
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：7S particles containing 5S RNA and the transcription regulatory protein factor A have been purified to near homogeneity from Xenopus laevis oocytes. The binding of the transcription factor to the Xenopus borealis somatic 5S RNA gene has been monitored by quantitating the DNase I protection patterns of the protein-DNA interaction. Under stoichiometric binding conditions--i.e., when all added DNA binds to the factor--two protein molecules are required to saturate the 5S RNA gene. Under equilibrium binding conditions, titration of the 5S RNA gene with factor A results in a sigmoidal binding isotherm suggesting a cooperative interaction; half-saturation of binding is observed at a free factor A concentration of 1 nM. Cooperative binding between factor A and the 5S RNA gene may contribute to the stability of the transcription apparatus and its maintenance during cell division.
