Transcribing <scp>RNA</scp> polymerase <scp>III</scp> observed by electron cryomicroscopy

Hoffmann, N.A.; Jakobi, Arjen J.; Vorländer, Matthias K.; Sachse, Carsten; Müller, Christoph W.

doi:10.1111/febs.13732

Cited by 17 publications

(13 citation statements)

References 50 publications

(65 reference statements)

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“…The rpc128-1007 allele is cold-sensitive due to a Gly1007Ala mutation at a buried interface between Rpc128 and AC40, a subunit that is shared between Pols I and III (Fig. 1B) [30]. The position of this mutation in the structure of Pol III suggests a specific assembly/stability defect.…”

Section: Metabolic Connections To Pol III and Maf1 In Yeastmentioning

confidence: 99%

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Maf1 phenotypes and cell physiology

Willis

2018

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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As a master regulator of transcription by RNA polymerase (Pol) III, Maf1 represses the synthesis of highly abundant non-coding RNAs as anabolic signals dissipate, as the quality or quantity of nutrients decreases, and under a wide range of cellular and environmental stress conditions. Thus, Maf1 responds to changes in cell physiology to conserve metabolic energy and to help maintain appropriate levels of tRNAs and other essential non-coding RNAs. Studies in different model organisms and cell-based systems show that perturbations of Maf1 can also impact cell physiology and metabolism. These effects are mediated by changes in Pol III transcription and/or by effects of Maf1 on the expression of select Pol II-transcribed genes. Maf1 phenotypes can vary between different systems and are sometimes conflicting as in comparisons between Maf1 KO mice and cultured mammalian cells. These studies are reviewed in an effort to better appreciate the relationship between Maf1 function and cell physiology. 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.

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Section: Metabolic Connections To Pol III and Maf1 In Yeastmentioning

confidence: 99%

“…Key functions of sugars in the upper part of the pathway are indicated as discussed in the text. B Top view of the Pol III elongating complex [30]. The boxed region, enlarged below, shows the position of the rpc128-1007 mutation in green and residues containing atoms within 5 Å.…”

Section: Figmentioning

confidence: 99%

Maf1 phenotypes and cell physiology

Willis

2018

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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“…subunit utilizing its eWH1 and eWH14 domains to anchor the Rpc82/34/31 subcomplex on the clamp domain of Rpc160 (6,7,12,13). The positioning of the Rpc82/34/31 subcomplex explains its functional contribution to transcription initiation (14)(15)(16)(17).…”

mentioning

confidence: 99%

“…According to cryo-EM structural analysis (5), the WH3 fold and the acidic C terminus are bound, respectively, to the eWH4 and coiled-coil domains of Rpc82. Due to structural flexibility, the tWH domain has not been resolved by cryo-EM (6,7,13,18) but, based on a chemical cross-linking study (19), it has been proposed that the domain is positioned directly above the cleft to interact with the transcription bubble. Functional insights into the tWH domain have come from a mutational analysis in which mutations of charged residues in the WH2 fold were found to severely compromise DNA melting in transcription initiation (17).…”

mentioning

confidence: 99%

Functions of the TFIIE-Related Tandem Winged-Helix Domain of Rpc34 in RNA Polymerase III Initiation and Elongation

Wei

Chen

2018

Molecular and Cellular Biology

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Rpc34 is a subunit of the Rpc82/34/31 subcomplex residing on the DNA-binding cleft of RNA polymerase (Pol) III. Rpc34 contains a structurally flexible N-terminal tandem winged-helix (tWH) domain related to the TFIIE transcription factor. While the second WH (WH2) fold of the tWH domain is known to function in DNA melting activity during transcription initiation, the functional role of the WH1 fold is unknown. In this study, we generated a series of new Rpc34 tWH mutants conferring a cold-sensitive growth phenotype. We found that the tWH mutations severely compromised transcription activity due to destabilization of the preinitiation complex (PIC). Site-specific protein photo-cross-linking analysis indicated that the tWH domain persistently interacts with protein subunits of the Pol III cleft in the PIC and the ternary elongation complex (TEC). Furthermore, purified Pol III proteins with tWH mutations also showed reduced efficiency in RNA elongation. Our study results suggest that the tWH domain is an important protein module above the Pol III cleft that integrates protein and nucleic acid interactions for initiation and elongation.

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“…Genes transcribed by RNA Pol III are involved in ribosome biogenesis, RNA processing, and chromatin regulation (Willis and Moir, 2018). RNA Pol III is a large complex (Hoffmann et al, 2016), in which transcription factor IIIB (TFIIIB) is a central transcription initiation unit. TFIIIB is composed of three proteins: TATA-binding protein (TBP), TFIIIB-related factor (BRF), and B-double prime 1 (BDP1) (Khoo et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

BRF Negatively Regulates Thermotolerance Defect of fes1a in Arabidopsis

Liu

et al. 2020

Front. Plant Sci.

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FES1A is a heat shock protein 70 binding protein. Mutation of FES1A leads to a defect in thermotolerance of Arabidopsis; however, independent fes1a mutants exhibit a range in the extent of thermosensitivity. Here, we found that BRF2, a gene adjacent to FES1A and encoding a component of transcription factor IIIB, affects the thermosensitivity of fes1a mutants. Knockout of BRF2 suppressed fes1a thermosensitivity, while overexpression of BRF2 increased thermosensitivity of fes1a. BRF2 in fes1a mutants regulates the transcriptional strength of RNA Polymerase II and accumulation of heat shock proteins and eventually affects the thermotolerance of fes1a. There is a cross-talking between RNA Pol III and Pol II. The cross-talking is initiated by BRF, magnified by the mutation of FES1A, and finally has an effect on thermotolerance.

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Transcribing RNA polymerase III observed by electron cryomicroscopy

Cited by 17 publications

References 50 publications

Maf1 phenotypes and cell physiology

Maf1 phenotypes and cell physiology

Functions of the TFIIE-Related Tandem Winged-Helix Domain of Rpc34 in RNA Polymerase III Initiation and Elongation

BRF Negatively Regulates Thermotolerance Defect of fes1a in Arabidopsis

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