Structural rearrangements of the RNA polymerase III machinery during tRNA transcription initiation

被引:19
|
作者
Ramsay, Ewan Phillip [1 ]
Vannini, Alessandro [1 ]
机构
[1] Inst Canc Res, London SW7 3RP, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
TFIIIC; TFIIIB; Brf2; RNA polymerase III; Transcription initiation; Facilitated recycling; TATA-BINDING PROTEIN; REPEAT-CONTAINING SUBUNIT; OCT-1 POU DOMAIN; HUMAN U6 GENE; SACCHAROMYCES-CEREVISIAE; TETRATRICOPEPTIDE REPEAT; FACTOR-TFIIIB; FACTOR-TAU; IN-VITRO; PREINITIATION COMPLEX;
D O I
10.1016/j.bbagrm.2017.11.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
RNA polymerase III catalyses the synthesis of tRNAs in eukaryotic organisms. Through combined biochemical and structural characterisation, multiple auxiliary factors have been identified alongside RNA Polymerase ill as critical in both facilitating and regulating transcription. Together, this machinery forms dynamic multi-protein complexes at tRNA genes which are required for polymerase recruitment, DNA opening and initiation and elongation of the tRNA transcripts. Central to the function of these complexes is their ability to undergo multiple conformational changes and rearrangements that regulate each step. Here, we discuss the available biochemical and structural data on the structural plasticity of multi-protein complexes involved in RNA Polymerase III transcriptional initiation and facilitated re-initiation during tRNA synthesis. Increasingly, structural information is becoming available for RNA polymerase III and its functional complexes, allowing for a deeper understanding of tRNA transcriptional initiation. This article is part of a Special Issue entitled: SI: Regulation of tRNA synthesis and modification in physiological conditions and disease edited by Dr. Boguta Magdalena.
引用
收藏
页码:285 / 294
页数:10
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