| Literature DB >> 29155071 |
Ewan Phillip Ramsay1, Alessandro Vannini2.
Abstract
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 III 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. CrownKeywords: Brf2; Facilitated recycling; RNA polymerase III; TFIIIB; TFIIIC; Transcription initiation
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Year: 2017 PMID: 29155071 DOI: 10.1016/j.bbagrm.2017.11.005
Source DB: PubMed Journal: Biochim Biophys Acta Gene Regul Mech ISSN: 1874-9399 Impact factor: 4.490