Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target

被引:33
作者
Todone, F
Weinzierl, ROJ
Brick, P
Onesti, S
机构
[1] Univ London Imperial Coll Sci Technol & Med, Blackett Lab, London SW7 2AZ, England
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AZ, England
基金
英国惠康基金;
关键词
D O I
10.1073/pnas.97.12.6306
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
Eukaryotic: nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12-18 different subunits, The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs, Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae. The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H, RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP(II) basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis a virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed alpha-helical structures.
引用
收藏
页码:6306 / 6310
页数:5
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