scholarly journals Reprogramming of mRNA expression in response to a defect in RNA polymerase III assembly in yeast Saccharomyces cerevisiae

2020 ◽  
Author(s):  
Izabela Rudzińska
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Mrna Expression ◽  
Rna Polymerase Iii ◽  
Yeast Saccharomyces Cerevisiae ◽  
Polymerase Iii

scholarly journals Defective RNA polymerase III is negatively regulated by the SUMO-Ubiquitin-Cdc48 pathway

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Zheng Wang ◽  
Catherine Wu ◽  
Aaron Aslanian ◽  
John R Yates ◽  
Tony Hunter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Regulatory Mechanism ◽  
Rna Polymerase Iii ◽  
Post Translational Modification ◽  
Yeast Saccharomyces Cerevisiae ◽  
Pol Ii ◽  
Polymerase Iii ◽  
Defective Rna ◽  
Pol Iii

Transcription by RNA polymerase III (Pol III) is an essential cellular process, and mutations in Pol III can cause neurodegenerative disease in humans. However, in contrast to Pol II transcription, which has been extensively studied, the knowledge of how Pol III is regulated is very limited. We report here that in budding yeast, Saccharomyces cerevisiae, Pol III is negatively regulated by the Small Ubiquitin-like MOdifier (SUMO), an essential post-translational modification pathway. Besides sumoylation, Pol III is also targeted by ubiquitylation and the Cdc48/p97 segregase; these three processes likely act in a sequential manner and eventually lead to proteasomal degradation of Pol III subunits, thereby repressing Pol III transcription. This study not only uncovered a regulatory mechanism for Pol III, but also suggests that the SUMO and ubiquitin modification pathways and the Cdc48/p97 segregase can be potential therapeutic targets for Pol III-related human diseases.

scholarly journals Casein kinase II is required for efficient transcription by RNA polymerase III.

1996 ◽  
Vol 16 (3) ◽  
pp. 892-898 ◽  
Author(s):  
D J Hockman ◽  
M C Schultz
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Rna Polymerases ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
Polymerase Iii

Casein kinase II (CKII) is a ubiquitous and highly conserved serine/threonine protein kinase found in the nucleus and cytoplasm of most cells. Using a combined biochemical and genetic approach in the yeast Saccharomyces cerevisiae, we assessed the role of CKII in specific transcription by RNA polymerases I, II, and III. CKII is not required for basal transcription by RNA polymerases I and II but is important for polymerase III transcription. Polymerase III transcription is high in extracts with normal CKII activity but low in extracts from a temperature-sensitive mutant that has decreased CKII activity due to a lesion in the enzyme's catalytic alpha' subunit. Polymerase III transcription of 5S rRNA and tRNA templates in the temperature-sensitive extract is rescued by purified, wild-type CKII. An inhibitor of CKII represses polymerase III transcription in wild-type extract, and this repression is partly overcome by supplementing reaction mixtures with active CKII. Finally, we show that polymerase III transcription in vivo is impaired when CKII is inactivated. Our results demonstrate that CKII, an oncogenic protein kinase previously implicated in cell cycle and growth control, is required for high-level transcription by RNA polymerase III.

scholarly journals Inactivation of the protein phosphatase 2A regulatory subunit A results in morphological and transcriptional defects in Saccharomyces cerevisiae

1992 ◽  
Vol 12 (11) ◽  
pp. 4946-4959
Author(s):  
W van Zyl ◽  
W Huang ◽  
A A Sneddon ◽  
M Stark ◽  
S Camier ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Rna Polymerase Iii ◽  
Regulatory Subunit ◽  
Predicted Amino Acid Sequence ◽  
Major Protein ◽  
Polymerase Iii ◽  
Phosphatase 2A

We have determined that TPD3, a gene previously identified in a screen for mutants defective in tRNA biosynthesis, most likely encodes the A regulatory subunit of the major protein phosphatase 2A species in the yeast Saccharomyces cerevisiae. The predicted amino acid sequence of the product of TPD3 is highly homologous to the sequence of the mammalian A subunit of protein phosphatase 2A. In addition, antibodies raised against Tpd3p specifically precipitate a significant fraction of the protein phosphatase 2A activity in the cell, and extracts of tpd3 strains yield a different chromatographic profile of protein phosphatase 2A than do extracts of isogenic TPD3 strains. tpd3 deletion strains generally grow poorly and have at least two distinct phenotypes. At reduced temperatures, tpd3 strains appear to be defective in cytokinesis, since most cells become multibudded and multinucleate following a shift to 13 degrees C. This is similar to the phenotype obtained by overexpression of the protein phosphatase 2A catalytic subunit or by loss of CDC55, a gene that encodes a protein with homology to a second regulatory subunit of protein phosphatase 2A. At elevated temperatures, tpd3 strains are defective in transcription by RNA polymerase III. Consistent with this in vivo phenotype, extracts of tpd3 strains fail to support in vitro transcription of tRNA genes, a defect that can be reversed by addition of either purified RNA polymerase III or TFIIIB. These results reinforce the notion that protein phosphatase 2A affects a variety of biological processes in the cell and provide an initial identification of critical substrates for this phosphatase.

scholarly journals Inactivation of the protein phosphatase 2A regulatory subunit A results in morphological and transcriptional defects in Saccharomyces cerevisiae.

1992 ◽  
Vol 12 (11) ◽  
pp. 4946-4959 ◽  
Author(s):  
W van Zyl ◽  
W Huang ◽  
A A Sneddon ◽  
M Stark ◽  
S Camier ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Rna Polymerase Iii ◽  
Regulatory Subunit ◽  
Predicted Amino Acid Sequence ◽  
Major Protein ◽  
Polymerase Iii ◽  
Phosphatase 2A

We have determined that TPD3, a gene previously identified in a screen for mutants defective in tRNA biosynthesis, most likely encodes the A regulatory subunit of the major protein phosphatase 2A species in the yeast Saccharomyces cerevisiae. The predicted amino acid sequence of the product of TPD3 is highly homologous to the sequence of the mammalian A subunit of protein phosphatase 2A. In addition, antibodies raised against Tpd3p specifically precipitate a significant fraction of the protein phosphatase 2A activity in the cell, and extracts of tpd3 strains yield a different chromatographic profile of protein phosphatase 2A than do extracts of isogenic TPD3 strains. tpd3 deletion strains generally grow poorly and have at least two distinct phenotypes. At reduced temperatures, tpd3 strains appear to be defective in cytokinesis, since most cells become multibudded and multinucleate following a shift to 13 degrees C. This is similar to the phenotype obtained by overexpression of the protein phosphatase 2A catalytic subunit or by loss of CDC55, a gene that encodes a protein with homology to a second regulatory subunit of protein phosphatase 2A. At elevated temperatures, tpd3 strains are defective in transcription by RNA polymerase III. Consistent with this in vivo phenotype, extracts of tpd3 strains fail to support in vitro transcription of tRNA genes, a defect that can be reversed by addition of either purified RNA polymerase III or TFIIIB. These results reinforce the notion that protein phosphatase 2A affects a variety of biological processes in the cell and provide an initial identification of critical substrates for this phosphatase.

scholarly journals Coupling of RNA polymerase III assembly to cell cycle progression in Saccharomyces cerevisiae

Cell Cycle ◽  
2019 ◽  
Vol 18 (4) ◽  
pp. 500-510
Author(s):  
Marta Płonka ◽  
Donata Wawrzycka ◽  
Robert Wysocki ◽  
Magdalena Boguta ◽  
Małgorzata Cieśla
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Rna Polymerase ◽  
Cell Cycle Progression ◽  
Rna Polymerase Iii ◽  
Cycle Progression ◽  
Polymerase Iii

scholarly journals Rbs1, a New Protein Implicated in RNA Polymerase III Biogenesis in Yeast Saccharomyces cerevisiae

2015 ◽  
Vol 35 (7) ◽  
pp. 1169-1181 ◽  
Author(s):  
Małgorzata Cieśla ◽  
Ewa Makała ◽  
Marta Płonka ◽  
Rafał Bazan ◽  
Kamil Gewartowski ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
De Novo ◽  
Rna Polymerase Iii ◽  
Growth Defect ◽  
Yeast Saccharomyces Cerevisiae ◽  
Content Type ◽  
Polymerase Iii ◽  
Cold Sensitive ◽  
Pol Iii ◽  
Synthetic Growth

Little is known about the RNA polymerase III (Pol III) complex assembly and its transport to the nucleus. We demonstrate that a missense cold-sensitive mutation,rpc128-1007, in the sequence encoding the C-terminal part of the second largest Pol III subunit, C128, affects the assembly and stability of the enzyme. The cellular levels and nuclear concentration of selected Pol III subunits were decreased inrpc128-1007cells, and the association between Pol III subunits as evaluated by coimmunoprecipitation was also reduced. To identify the proteins involved in Pol III assembly, we performed a genetic screen for suppressors of therpc128-1007mutation and selected the Rbs1 gene, whose overexpression enhancedde novotRNA transcription inrpc128-1007cells, which correlated with increased stability, nuclear concentration, and interaction of Pol III subunits. Therpc128-1007 rbs1Δ double mutant shows a synthetic growth defect, indicating thatrpc128-1007andrbs1Δ function in parallel ways to negatively regulate Pol III assembly. Rbs1 physically interacts with a subset of Pol III subunits, AC19, AC40, and ABC27/Rpb5. Additionally, Rbs1 interacts with the Crm1 exportin and shuttles between the cytoplasm and nucleus. We postulate that Rbs1 binds to the Pol III complex or subcomplex and facilitates its translocation to the nucleus.

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