Wong J M, Liu F, Bateman E
Department of Microbiology and Molecular Genetics, University of Vermont, Burlington 05405-0068.
Gene. 1992 Aug 1;117(1):91-7. doi: 10.1016/0378-1119(92)90494-a.
We have cloned and characterized the cDNA encoding transcription factor TFIID from the eukaryote, Acanthamoeba castellanii. The gene occurs as a single species, encodes one mRNA and, presumably, a single protein. A. castellanii TFIID contains two recognizable domains, a nonconserved N-terminal domain and a highly conserved C-terminal domain. Similarities between the amino acid (aa) sequences of TFIID from several organisms are also found within the N-terminal 78 aa, suggesting a potential role in TFIID function. Full-length or truncated A. castellanii TFIID produced in Escherichia coli binds to a TATA box and is able to activate transcription in a TFIID-depleted HeLa cell extract, but the C-terminal 180-aa domain was found to be less efficient in these reactions.
我们已经克隆并鉴定了真核生物卡氏棘阿米巴中编码转录因子TFIID的cDNA。该基因以单一形式存在,编码一种mRNA,推测也编码一种单一蛋白质。卡氏棘阿米巴TFIID包含两个可识别的结构域,一个非保守的N端结构域和一个高度保守的C端结构域。在几种生物的TFIID氨基酸(aa)序列之间的相似性也在N端78个aa内被发现,这表明其在TFIID功能中具有潜在作用。在大肠杆菌中产生的全长或截短的卡氏棘阿米巴TFIID与TATA框结合,并能够在TFIID缺失的HeLa细胞提取物中激活转录,但发现C端180个aa的结构域在这些反应中的效率较低。