DNA binding domain and subunit interactions of transcription factor IIIC revealed by dissection with poliovirus 3C protease.
DNA binding domain and subunit interactions of transcription factor IIIC revealed by dissection with poliovirus 3C protease.
复制标题
通过脊髓灰质炎病毒 3C 蛋白酶解剖揭示转录因子 IIIC 的 DNA 结合域和亚基相互作用。
DOI：
10.1128/mcb.16.8.4163
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发表时间：
1996
影响因子：
5.3
通讯作者：
Dasgupta,A
中科院分区：
文献类型：
--
作者：
Shen,Y;Igo,M;Yalamanchili,P;Berk,AJ;Dasgupta,A
Transcription factor IIIC (TFIIIC) is a general RNA polymerase III transcription factor that binds the B-box internal promotor element of tRNA genes and the complex of TFIIIA with a 5S rRNA gene. TFIIIC then directs the binding of TFIIIB to DNA upstream of the transcription start site. TFIIIB in turn directs RNA polymerase III binding and initiation. Human TFIIIC contains five different subunits. The 243-kDa α subunit can be specifically cross-linked to B-box DNA, but its sequence does not reveal a known DNA binding domain. During poliovirus infection, TFIIIC is cleaved and inactivated by the poliovirus-encoded 3C protease (3Cpro). Here we analyzed the cleavage of TFIIIC subunits by 3Cpro in vitro and during poliovirus infection of HeLa cells. Analyses of the DNA binding activities of the resulting subcomplexes indicated that an N-terminal 83-kDa domain of the α subunit associates with the β subunit to generate the TFIIIC DNA binding domain. Cleavage with 3Cpro also generated an ~125-kBA;Da C-terminal fragment of the α subunit which remained associated with the γ and ε subunits.
