5 SWI/SNF GENE-PRODUCTS ARE COMPONENTS OF A LARGE MULTISUBUNIT COMPLEX REQUIRED FOR TRANSCRIPTIONAL ENHANCEMENT

5 SWI/SNF GENE-PRODUCTS ARE COMPONENTS OF A LARGE MULTISUBUNIT COMPLEX REQUIRED FOR TRANSCRIPTIONAL ENHANCEMENT
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DOI:
10.1073/pnas.91.8.2905
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发表时间:
1994-04-12
影响因子:
11.1
通讯作者:
SCOTT, MP
SCOTT, MP
中科院分区:
综合性期刊1区
文献类型:
--
作者:
PETERSON, CL;DINGWALL, A;SCOTT, MP

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酿酒酵母SW11、SWI2 (SNF2)、SWI3、SNFS和SNF6基因产物在转录调控中起着至关重要的作用。我们在这里提供了直接的生化证据,证明所有河流SWI/SNF多肽都是一个大的多亚基复合物的组成部分。这五种多肽从凝胶过滤柱中析出,其表观分子质量几乎等于2 MDa。当从SWI -或SNF -突变体中提取提取物时,这5种SWI/SNF多肽不会发生聚合。我们发现SWI/SNF多肽在亲和色谱步骤之后的凝胶过滤过程中也保持关联。SWI/SNF复合物的组装不会因SWI2的假定atp结合位点突变而中断,尽管这种突变消除了SWI2的功能。
The Saccharomyces cerevisiae SW11, SWI2 (SNF2), SWI3, SNFS, and SNF6 gene products play a crucial role in the regulation of transcription. We provide here direct biochemical evidence that all rive SWI/SNF polypeptides are components of a large multisubunit complex. These five polypeptides coelute from a gel-filtration column with an apparent molecular mass of almost-equal-to 2 MDa. The five SWI/SNF polypeptides do not copurify when extracts are prepared from swi- or snf- mutants. We show that SWI/SNF polypeptides also remain associated during an affinity-chromatography step followed by gel filtration. Assembly of the SWI/SNF complex is not disrupted by a mutation in the putative ATP-binding site of SWI2, although this mutation eliminates SWI2 function.