A facelift for the general transcription factor TFIIA

Torill Høiby , Huiqing Zhou , Dimitra J. Mitsiou , Hendrik G. Stunnenberg
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引用次数: 48

Abstract

TFIIA was classified as a general transcription factor when it was first identified. Since then it has been debated to what extent it can actually be regarded as “general”. The most notable feature of TFIIA is the proteolytical cleavage of the TFIIAαβ into a TFIIAα and TFIIAβ moiety which has long remained a mystery. Recent studies have showed that TFIIA is cleaved by Taspase1 which was initially identified as the protease for the proto-oncogene MLL. Cleavage of TFIIA does not appear to serve as a step required for its activation as the uncleaved TFIIA in the Taspase1 knock-outs adequately support bulk transcription. Instead, cleavage of TFIIA seems to affect its turn-over and may be a part of an intricate degradation mechanism that allows fine-tuning of cellular levels of TFIIA. Cleavage might also be responsible for switching transcription program as the uncleaved and cleaved TFIIA might have distinct promoter specificity during development and differentiation. This review will focus on functional characteristics of TFIIA and discuss novel insights in the role of this elusive transcription factor.

对一般转录因子TFIIA的改进
TFIIA最初被发现时被归类为一般转录因子。从那时起,人们一直在争论,在多大程度上它实际上可以被视为“一般”。TFIIA最显著的特征是TFIIAαβ的蛋白水解裂解成TFIIAα和TFIIAβ片段,这一直是一个谜。最近的研究表明TFIIA被Taspase1切割,Taspase1最初被鉴定为原癌基因MLL的蛋白酶。TFIIA的切割似乎不是其激活所需的步骤,因为Taspase1敲除中未切割的TFIIA充分支持批量转录。相反,TFIIA的切割似乎会影响其翻转,并且可能是复杂降解机制的一部分,该机制允许微调TFIIA的细胞水平。裂解也可能导致转录程序的切换,因为未裂解和裂解的TFIIA在发育和分化过程中可能具有不同的启动子特异性。本文将重点介绍TFIIA的功能特征,并讨论这一难以捉摸的转录因子的新作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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