TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription fac

TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription fac
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TATA 盒结合蛋白 (TBP) 是与 rRNA 启动子结合的聚合酶 I 特异性转录起始因子 TIF-IB (SL1) 的组成部分,并且在聚合酶 I、II 和 III 转录因子中对 TBP 导向试剂表现出不同的敏感性

DOI:
10.1128/mcb.14.1.597-605.1994
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发表时间:
1994
影响因子:
5.3
通讯作者:
Paule,MR
Paule,MR
中科院分区:
生物学2区
文献类型:
--
作者:
Radebaugh,CA;Matthews,JL;Geiss,GK;Liu,F;Wong,JM;Bateman,E;Camier,S;Sentenac,A;Paule,MR

文献摘要

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研究了棘阿米巴castellaniitata结合蛋白(TBP)在转录中的作用。针对TBP的非保守n端结构域的特异性抗体被用来验证TBP在RNA聚合酶I的基本转录起始因子TIF-IB中的存在,并证明TBP是rRNA启动子上承诺起始复合物的一部分。同样的抗体在所有三种聚合酶系统中抑制转录,但它们的作用不同。寡核苷酸竞争对手被用来评估tfi - ib、TFIID和TFIIIB中tata结合位点的可及性。结果表明,TBP插入聚合酶II和III因子比插入聚合酶I因子更相似。
The role of theAcanthamoeba castellaniiTATA-binding protein (TBP) in transcription was examined. Specific antibodies against the nonconserved N-terminal domain of TBP were used to verify the presence of TBP in the fundamental transcription initiation factor for RNA polymerase I, TIF-IB, and to demonstrate that TBP is part of the committed initiation complex on the rRNA promoter. The same antibodies inhibit transcription in all three polymerase systems, but they do so differentially. Oligonucleotide competitors were used to evaluate the accessibility of the TATA-binding site in TIF-IB, TFIID, and TFIIIB. The results suggest that insertion of TBP into the polymerase II and III factors is more similar than insertion into the polymerase I factor.