scholarly journals RNA Polymerase II CTD phosphatase Rtr1 fine-tunes transcription termination

PLoS Genetics ◽  
2020 ◽  
Vol 16 (3) ◽  
pp. e1008317 ◽  
Author(s):  
Jose F. Victorino ◽  
Melanie J. Fox ◽  
Whitney R. Smith-Kinnaman ◽  
Sarah A. Peck Justice ◽  
Katlyn H. Burriss ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Termination ◽  
Ctd Phosphatase ◽  
Rna Polymerase Ii Ctd

scholarly journals The Structure of Fcp1, an Essential RNA Polymerase II CTD Phosphatase

2008 ◽  
Vol 32 (4) ◽  
pp. 478-490 ◽  
Author(s):  
Agnidipta Ghosh ◽  
Stewart Shuman ◽  
Christopher D. Lima
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Ctd Phosphatase ◽  
Rna Polymerase Ii Ctd

Inhibition of Tat transactivation by the RNA polymerase II CTD-phosphatase FCP1

AIDS ◽  
2001 ◽  
Vol 15 (3) ◽  
pp. 301-307 ◽  
Author(s):  
Paolo Licciardo ◽  
Giuliana Napolitano ◽  
Barbara Majello ◽  
Luigi Lania
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Ctd Phosphatase ◽  
Rna Polymerase Ii Ctd

scholarly journals Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1

RNA ◽  
2015 ◽  
Vol 21 (6) ◽  
pp. 1135-1146 ◽  
Author(s):  
Beate Schwer ◽  
Agnidipta Ghosh ◽  
Ana M. Sanchez ◽  
Christopher D. Lima ◽  
Stewart Shuman
Keyword(s):  
Structural Analysis ◽  
Rna Polymerase ◽  
Fission Yeast ◽  
Rna Polymerase Ii ◽  
Ctd Phosphatase ◽  
Rna Polymerase Ii Ctd

scholarly journals Ssu72 Is an RNA Polymerase II CTD Phosphatase

2004 ◽  
Vol 14 (3) ◽  
pp. 387-394 ◽  
Author(s):  
Shankarling Krishnamurthy ◽  
Xiaoyuan He ◽  
Mariela Reyes-Reyes ◽  
Claire Moore ◽  
Michael Hampsey
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Ctd Phosphatase ◽  
Rna Polymerase Ii Ctd

Regulation of transcription by an RNA polymerase II CTD phosphatase

1999 ◽  
Vol 77 (4) ◽  
pp. 398
Author(s):  
Michael S Kobor ◽  
Jacques Archambault ◽  
David Jansma ◽  
William Lester ◽  
Lisa Simon ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Regulation Of Transcription ◽  
Ctd Phosphatase ◽  
Rna Polymerase Ii Ctd

scholarly journals RNA Polymerase II CTD phosphatase Rtr1 prevents premature transcription termination

2019 ◽  
Author(s):  
Melanie J. Fox ◽  
Jose F. Victorino ◽  
Whitney R. Smith-Kinnaman ◽  
Sarah A. Peck Justice ◽  
Hongyu Gao ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Binding ◽  
Premature Termination ◽  
Transcription Termination ◽  
Noncoding Rnas ◽  
Termination Factor ◽  
Protein Coding ◽  
Protein Coding Genes ◽  
Ctd Phosphatase

ABSTRACTRNA Polymerase II (RNAPII) transcription termination is regulated by the phosphorylation status of the C-terminal domain (CTD). Using disruption-compensation (DisCo) protein-protein interaction network analysis, interaction changes were observed within the termination machinery as a consequence of deletion of the serine 5 RNAPII CTD phosphatase Rtr1. Interactions between RNAPII and the cleavage factor IA (CF1A) subunit Pcf11 were reduced in rtr1Δ, whereas interactions with the CTD and RNA-binding termination factor Nrd1 were increased. These changes could be the result of altered interactions between the termination machinery and/or increased levels of premature termination of RNAPII. Transcriptome analysis in rtr1Δ cells found decreased pervasive transcription and a shift in balance of expression of sense and antisense transcripts. Globally, rtr1Δ leads to decreases in noncoding RNAs that are linked to the Nrd1, Nab3 and Sen1 (NNS)-dependent RNAPII termination pathway. Genome-wide analysis of RNAPII and Nrd1 occupancy suggests that loss of RTR1 leads to increased termination at noncoding genes and increased efficiency of snRNA termination. Additionally, premature termination increases globally at protein-coding genes where NNS is recruited during early elongation. The effects of rtr1Δ on RNA expression levels were erased following deletion of the exosome subunit Rrp6, which works with the NNS complex to rapidly degrade terminated noncoding RNAs. Overall, these data suggest that Rtr1 restricts the NNS-dependent termination pathway in WT cells to prevent premature RNAPII termination of mRNAs and ncRNAs. Additionally, Rtr1 phosphatase activity facilitates low-level elongation of noncoding transcripts that impact the transcriptome through RNAPII interference.AUTHOR SUMMARYMany cellular RNAs including those that encode for proteins are produced by the enzyme RNA Polymerase II. In this work, we have defined a new role for the phosphatase Rtr1 in the regulation of RNA Polymerase II progression from the start of transcription to the 3’ end of the gene where the nascent RNA from protein-coding genes is typically cleaved and polyadenylated. Deletion of the gene that encodes RTR1 leads to changes in the interactions between RNA polymerase II and the termination machinery. Rtr1 loss also causes early termination of RNA Polymerase II at many of its target gene types including protein coding genes and noncoding RNAs. Evidence suggests that the premature termination observed in RTR1 knockout cells occurs through the termination factor and RNA binding protein Nrd1 and its binding partner Nab3. Additionally, many of the prematurely terminated noncoding RNA transcripts are degraded by the Rrp6-containing nuclear exosome, a known component of the Nrd1-Nab3 termination coupled RNA degradation pathway. These findings suggest that Rtr1 normally promotes elongation of RNA Polymerase II transcripts through preventation of Nrd1-directed termination.

scholarly journals Identification of three sequence motifs in the transcription termination factor Sen1 that mediate direct interactions with Nrd1

2018 ◽  
Author(s):  
Yinglu Zhang ◽  
Yujin Chun ◽  
Stephen Buratowski ◽  
Liang Tong
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Termination ◽  
Noncoding Rnas ◽  
Sequence Motifs ◽  
Interaction Domain ◽  
Termination Factor ◽  
Transcription Termination Factor ◽  
Rna Polymerase Ii Ctd

AbstractThe Nrd1-Nab3-Sen1 (NNS) complex carries out the transcription termination of noncoding RNAs (ncRNAs) in yeast, although the detailed interactions among its subunits remain obscure. Here we have identified three sequence motifs in Sen1 that mediate direct interactions with the RNA polymerase II CTD interaction domain (CID) of Nrd1, determined the crystal structures of these Nrd1 interaction motifs (NIMs) bound to the CID, and characterized the interactions in vitro and in yeast.

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