Genetics of eukaryotic RNA polymerases I, II, and III.

Archambault, Jacques; Friesen, James D.

doi:10.1128/mmbr.57.3.703-724.1993

Cited by 90 publications

(29 citation statements)

References 98 publications

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“…By convention, the subunits are named using 'RP' for RNAP, 'A', 'B' and 'C' for Pol I, II and III, respectively, and a number (starting from the largest) for the specific subunit; for example, RPA1 is the 1 st (largest) subunit for Pol I. Most yeast Pol II subunits are essential for cell viability, except for the 4 th (RPB4) and 9 th (RPB9) subunits (Archambault & Friesen, 1993;Hull et al, 1995;Sampath & Sadhale, 2005). Within the conserved core, five subunits (1 st , 2 nd , 3 rd , 9 th , 11 th ) are each encoded by a multigene family, having specific paralogs for Pol I, II and III, respectively (Cramer et The compositions of Pol II, IV and V subunits were from previous biochemical studies (Huang et al, 2009;Ream et al, 2009;Law et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Step‐wise and lineage‐specific diversification of plant RNA polymerase genes and origin of the largest plant‐specific subunits

Wang

Mā

2015

New Phytologist

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SummaryProteins often function as complexes, yet little is known about the evolution of dissimilar subunits of complexes. DNA-directed RNA polymerases (RNAPs) are multisubunit complexes, with distinct eukaryotic types for different classes of transcripts. In addition to Pol I-III, common in eukaryotes, plants have Pol IV and V for epigenetic regulation. Some RNAP subunits are specific to one type, whereas other subunits are shared by multiple types.We have conducted extensive phylogenetic and sequence analyses, and have placed RNAP gene duplication events in land plant history, thereby reconstructing the subunit compositions of the novel RNAPs during land plant evolution.We found that Pol IV/V have experienced step-wise duplication and diversification of various subunits, with increasingly distinctive subunit compositions. Also, lineage-specific duplications have further increased RNAP complexity with distinct copies in different plant families and varying divergence for subunits of different RNAPs. Further, the largest subunits of Pol IV/V probably originated from a gene fusion in the ancestral land plants.We propose a framework of plant RNAP evolution, providing an excellent model for protein complex evolution.

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Section: Introductionmentioning

confidence: 99%

Step‐wise and lineage‐specific diversification of plant RNA polymerase genes and origin of the largest plant‐specific subunits

Wang

Mā

2015

New Phytologist

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“…All channels have a highly positive surface and stabilize the nucleic acids by van der Waals and polar interactions between amino acid residues of the polymerase and the phosphate backbone of the DNA or RNA (Vassylyev et al, 2007). Unlike eukaryotic cells, which encode three distinct RNA polymerases, prokaryotes use only one RNA polymerase to produce rRNAs, mRNAs and tRNAs (Archambault and Friesen, 1993). This makes the bacterial RNA polymerase a fitness-determining enzyme since bacterial growth rate is directly related to the rate of production of rRNAs (Condon et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Fitness‐compensatory mutations in rifampicin‐resistant RNA polymerase

Brandis

Wrande

Liljas

et al. 2012

Molecular Microbiology

147

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Using Salmonella as a model organism, and a previously characterized Rif R mutation (rpoB R529C) as a starting point, independent lineages were evolved with selection for improved growth in the presence and absence of rifampicin. Compensatory mutations were identified in every lineage and were distributed between rpoA, rpoB and rpoC. Resistance was maintained in all strains showing that increased fitness by compensatory mutation was more likely than reversion. Genetic reconstructions demonstrated that the secondary mutations were responsible for increasing growth rate. Many of the compensatory mutations in rpoA and rpoC individually caused small but significant reductions in susceptibility to rifampicin, and some compensatory mutations in rpoB individually caused high-level resistance. These findings show that mutations in different components of RNA polymerase are responsible for fitness compensation of a Rif R mutant.

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“…DNA-dependent RNA polymerase (RNAp) is the vital enzyme in transcription and therefore the main target of transcriptional regulation. The multisubunit RNA polymerases of eukaryotes (Pols I, II and III), bacteria, archaea and chloroplasts exhibit unambiguous similarities in sequence, structure and function (Archambault and Friesen, 1993;Cramer et al, 2000). Therefore an understanding of the bacterial RNAp system provides an insight into the general mechanisms of all multisubunit RNAps.…”

Section: Introductionmentioning

confidence: 99%

Escherichia coli RNA polymerase core and holoenzyme structures

Finn¹

2000

The EMBO Journal

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Multisubunit RNA polymerase is an essential enzyme for regulated gene expression. Here we report two Escherichia coli RNA polymerase structures: an 11.0 A Ê structure of the core RNA polymerase and a 9.5 A Ê structure of the s 70 holoenzyme. Both structures were obtained by cryo-electron microscopy and angular reconstitution. Core RNA polymerase exists in an open conformation. Extensive conformational changes occur between the core and the holoenzyme forms of the RNA polymerase, which are largely associated with movements in b¢. All common RNA polymerase subunits (a 2 , b, b¢) could be localized in both structures, thus suggesting the position of s 70 in the holoenzyme.

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Genetics of eukaryotic RNA polymerases I, II, and III.

Cited by 90 publications

References 98 publications

Step‐wise and lineage‐specific diversification of plant RNA polymerase genes and origin of the largest plant‐specific subunits

Step‐wise and lineage‐specific diversification of plant RNA polymerase genes and origin of the largest plant‐specific subunits

Fitness‐compensatory mutations in rifampicin‐resistant RNA polymerase

Escherichia coli RNA polymerase core and holoenzyme structures

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