STIMULATION OF GAL4 DERIVATIVE BINDING TO NUCLEOSOMAL DNA BY THE YEAST SWI/SNF COMPLEX
STIMULATION OF GAL4 DERIVATIVE BINDING TO NUCLEOSOMAL DNA BY THE YEAST SWI/SNF COMPLEX
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DOI：
10.1126/science.8016655
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发表时间：
1994-07-01
期刊：
影响因子：
56.9
通讯作者：
PETERSON, CL
中科院分区：
文献类型：
--
作者：
COTE, J;QUINN, J;PETERSON, CL
SWI/SNF蛋白复合物是酵母中许多转录激活因子增强转录所必需的。在这里，它表明，纯化的SWI/SNF复合物由10个亚基组成，并包括SWI 1，SW 12/SNF 2，SWI 3，SNF 5和SNF 6基因产物。该复合物具有DNA刺激的腺苷三磷酸酶（ATP酶）活性，但缺乏解旋酶活性。SWI/SNF复合物在GAL 4衍生物与核小体DNA的结合反应中引起10- 30倍的刺激，该反应需要三磷酸腺苷（ATP）水解，但不依赖于激活结构域。刺激GAL 4结合的复合物被废除的突变SWI 2亚基，并增加了组蛋白结合蛋白，核质的存在。检测到SWI/SNF复合物与核小体DNA之间的直接ATP依赖性相互作用。这些观察结果表明，SWI/SNF复合物的主要作用是促进激活剂与核小体DNA的结合。
The SWI/SNF protein complex is required for the enhancement of transcription by many transcriptional activators in yeast. Here it is shown that the purified SWI/SNF complex is composed of 10 subunits and includes the SWI1, SW12/SNF2, SWI3, SNF5, and SNF6 gene products. The complex exhibited DNA-stimulated adenosine triphosphatase (ATPase) activity, but lacked helicase activity. The SWI/SNF complex caused a 10- to 30-fold stimulation in the binding of GAL4 derivatives to nucleosomal DNA in a reaction that required adenosine triphosphate (ATP) hydrolysis but was activation domain-independent. Stimulation of GAL4 binding by the complex was abolished by a mutant SWI2 subunit, and was increased by the presence of a histone-binding protein, nucleoplasmin. A direct ATP-dependent interaction between the SWI/SNF complex and nucleosomal DNA was detected. These observations suggest that a primary role of the SWI/SNF complex is to promote activator binding to nucleosomal DNA.