FUNCTIONAL DOMAINS OF TRANSCRIPTION FACTOR-TFIIB

被引:109
作者
BURATOWSKI, S
ZHOU, H
机构
[1] Whitehead Inst. for Biomed. Research, Nine Cambridge Center, Cambridge
关键词
RNA POLYMERASE-II; TRANSCRIPTION INITIATION; TATA-BINDING PROTEIN;
D O I
10.1073/pnas.90.12.5633
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Transcription factor TFIIB is an essential component of the RNA polymerase II initiation complex. TFIIB carries out at least two functions: it interacts directly with the TATA-binding protein (TBP) and helps to recruit RNA polymerase II into the initiation complex. The sequence of TFIIB reveals a potential zinc-binding domain and an imperfect duplication of almost-equal-to 70 amino acids. Mutagenesis of cysteine codons within the putative zinc finger results in mutant proteins that bind normally to TBP but are unable to recruit RNA polymerase II-TFIIF into the initiation complex. Changing the two most highly conserved amino acids in the TFIIB repeats reduces the ability of TFIIB to interact with TBP. Therefore, the two functions of TFIIB can be assigned to two separable functional domains of the protein.
引用
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页码:5633 / 5637
页数:5
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