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Abstract
Eukaryotic RNA polymerases (RNA pols) transcriptional processes have been extensively investigated, and the structural analysis of eukaryotic RNA pols has been explored. However, the global assembly and biogenesis of these heteromultimeric complexes have been narrowly studied. Despite nuclear transcription being carried out by three RNA polymerases in eukaryotes (five in plants) with specificity in the synthesis of different RNA types, the biogenesis process has been proposed to be similar, at least for RNA pol II, to that of bacteria, which contains only one RNA pol. The formation of three different interacting subassembly complexes to conform the complete enzyme in the cytoplasm, prior to its nuclear import, has been assumed. In Saccharomyces cerevisiae, recent studies have examined in depth the biogenesis of RNA polymerases by characterizing some elements involved in the assembly of these multisubunit complexes, some of which are conserved in humans. This study reviews the latest studies governing the mechanisms and proteins described as being involved in the biogenesis of RNA polymerases in yeast.
Highlights
Transcription is the most studied step of the gene expression catalyzed by RNA polymerases (RNA pols)
This review focuses on pre-existing knowledge of the assembly of RNA polymerases in yeast
In line with previously proposed mechanisms for yeast, quantitative proteomic analyses in human cells have demonstrated the existence of a cytoplasmic RNA pol II subcomplex formed by subunits RPB2, RPB3, RPB10, RPB11, and RPB12 (Boulon et al, 2010), which suggests that the interaction of the RPB2 and RPB3 subassembly complexes may occur prior to the association with the RPB1 subassembly complex
Summary
Transcription is the most studied step of the gene expression catalyzed by RNA polymerases (RNA pols). In line with previously proposed mechanisms for yeast, quantitative proteomic analyses in human cells have demonstrated the existence of a cytoplasmic RNA pol II subcomplex formed by subunits RPB2, RPB3, RPB10, RPB11, and RPB12 (Boulon et al, 2010), which suggests that the interaction of the RPB2 and RPB3 subassembly complexes may occur prior to the association with the RPB1 subassembly complex.
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