Purification and characterization of transcription factor IIIA from Acanthamoeba castellanii.
Purification and characterization of transcription factor IIIA from Acanthamoeba castellanii.
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卡斯氏棘阿米巴转录因子 IIIA 的纯化和表征。
DOI：
10.1093/nar/30.9.1977
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发表时间：
2002
影响因子：
14.9
通讯作者：
Paule,MarvinR
中科院分区：
文献类型：
--
作者：
Polakowski,Nicholas;Paule,MarvinR
TFIIIA是激活5S RNA基因的RNA聚合酶III转录所必需的。尽管所有已知的TFIIIA同源物都含有九个参与DNA结合的锌指，但这些蛋白质之间的序列同源性非常有限，这反映了一些TFIIIA同源物的独特性质。例如，卡氏棘阿米巴同系物直接调节5S RNA转录。为了更清楚地了解这些差异和调控过程，我们已经纯化并鉴定了A.CastellaniTFIIIA(AcTFIIIA)。AcTFIIIA全长59 kDa，明显大于迄今分离的所有其他TFIIIA同源物。然而，它表现出与较小脊椎动物TFIIIA同源物非常相似的DNase I足迹，但不同于酿酒酵母51 kDa TFIIIA的较小足迹。相似的足迹并没有反映在卡氏曲霉和脊椎动物启动子之间更大的序列相似性上。
TFIIIA is required to activate RNA polymerase III transcription from 5S RNA genes. Although all known TFIIIA homologs harbor nine zinc fingers that mediate DNA binding, very limited sequence homology is found among these proteins, which reflects unique properties of some TFIIIA homologs. For example, theAcanthamoeba castellaniihomolog directly regulates 5S RNA transcription. We have purified and characterizedA.castellaniiTFIIIA (AcTFIIIA) as a step toward obtaining a clearer understanding of these differences and of the regulatory process.AcTFIIIA is 59 kDa, significantly larger than all other TFIIIA homologs isolated to date. Nevertheless, it exhibits a DNase I footprint very similar to those produced by the smaller vertebrate TFIIIA homologs, but distinct from the smaller footprint of the 51 kDa TFIIIA fromSaccharomyces cerevisiae. Similar footprinting is not reflected in greater sequence similarity between theA.castellaniiand vertebrate promoters.