scholarly journals Mapping RNAPII CTD Phosphorylation Reveals That the Identity and Modification of Seventh Heptad Residues Direct Tyr1 Phosphorylation

2019 ◽  
Author(s):  
Nathaniel T. Burkholder ◽  
Sarah N. Sipe ◽  
Edwin E. Escobar ◽  
Mukeshkumar Venkatramani ◽  
Seema Irani ◽  
...  
Keyword(s):  
Ctd Phosphorylation

scholarly journals Sub1 Globally Regulates RNA Polymerase II C-Terminal Domain Phosphorylation

2010 ◽  
Vol 30 (21) ◽  
pp. 5180-5193 ◽  
Author(s):  
Alicia García ◽  
Emanuel Rosonina ◽  
James L. Manley ◽  
Olga Calvo
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Large Subunit ◽  
Terminal Domain ◽  
Mrna Metabolism ◽  
Genes Encoding ◽  
The One ◽  
Ctd Phosphorylation ◽  
Transcription Cycle

ABSTRACT The transcriptional coactivator Sub1 has been implicated in several aspects of mRNA metabolism in yeast, such as activation of transcription, termination, and 3′-end formation. Here, we present evidence that Sub1 plays a significant role in controlling phosphorylation of the RNA polymerase II large subunit C-terminal domain (CTD). We show that SUB1 genetically interacts with the genes encoding all four known CTD kinases, SRB10, KIN28, BUR1, and CTK1, suggesting that Sub1 acts to influence CTD phosphorylation at more than one step of the transcription cycle. To address this directly, we first used in vitro kinase assays, and we show that, on the one hand, SUB1 deletion increased CTD phosphorylation by Kin28, Bur1, and Ctk1 but, on the other, it decreased CTD phosphorylation by Srb10. Second, chromatin immunoprecipitation assays revealed that SUB1 deletion decreased Srb10 chromatin association on the inducible GAL1 gene but increased Kin28 and Ctk1 chromatin association on actively transcribed genes. Taken together, our data point to multiple roles for Sub1 in the regulation of CTD phosphorylation throughout the transcription cycle.

scholarly journals Nucleic Acid Content of HBV Capsids Depends on its CTD-Phosphorylation State

2013 ◽  
Vol 19 (S2) ◽  
pp. 54-55
Author(s):  
G. Tolun ◽  
N. Cheng ◽  
B.J. Heymann ◽  
P.T. Wingfield ◽  
L. Ludgate ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Acid Content ◽  
Nucleic Acid Content ◽  
Phosphorylation State ◽  
Ctd Phosphorylation

Extended abstract of a paper presented at Microscopy and Microanalysis 2013 in Indianapolis, Indiana, USA, August 4 – August 8, 2013.

scholarly journals RNA Pol II Dynamics Modulate Co-transcriptional Chromatin Modification, CTD Phosphorylation, and Transcriptional Direction

2017 ◽  
Vol 66 (4) ◽  
pp. 546-557.e3 ◽  
Author(s):  
Nova Fong ◽  
Tassa Saldi ◽  
Ryan M. Sheridan ◽  
Michael A. Cortazar ◽  
David L. Bentley
Keyword(s):  
Chromatin Modification ◽  
Rna Pol Ii ◽  
Pol Ii ◽  
Transcriptional Direction ◽  
Ctd Phosphorylation

scholarly journals Modulation of TFIIH-associated kinase activity by complex formation and its relationship with CTD phosphorylation of RNA polymerase II

2000 ◽  
Vol 5 (5) ◽  
pp. 407-423 ◽  
Author(s):  
Yoshinori Watanabe ◽  
Hiroyuki Fujimoto ◽  
Tomomichi Watanabe ◽  
Takafumi Maekawa ◽  
Chikahide Masutani ◽  
...  
Keyword(s):  
Complex Formation ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Kinase Activity ◽  
Ctd Phosphorylation

scholarly journals RNA Polymerase II Carboxy-Terminal Domain Phosphorylation Is Required for Cotranscriptional Pre-mRNA Splicing and 3′-End Formation

2004 ◽  
Vol 24 (20) ◽  
pp. 8963-8969 ◽  
Author(s):  
Gregory Bird ◽  
Diego A. R. Zorio ◽  
David L. Bentley
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Kinase Inhibitors ◽  
Mrna Splicing ◽  
Pol Ii ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal ◽  
Ctd Phosphorylation

ABSTRACT We investigated the role of RNA polymerase II (pol II) carboxy-terminal domain (CTD) phosphorylation in pre-mRNA processing coupled and uncoupled from transcription in Xenopus oocytes. Inhibition of CTD phosphorylation by the kinase inhibitors 5,6-dichloro-1β-d-ribofuranosyl-benzimidazole and H8 blocked transcription-coupled splicing and poly(A) site cleavage. These experiments suggest that pol II CTD phosphorylation is required for efficient pre-mRNA splicing and 3′-end formation in vivo. In contrast, processing of injected pre-mRNA was unaffected by either kinase inhibitors or α-amanitin-induced depletion of pol II. pol II therefore does not appear to participate directly in posttranscriptional processing, at least in frog oocytes. Together these experiments show that the influence of the phosphorylated CTD on pre-mRNA splicing and 3′-end processing is mediated by transcriptional coupling.

scholarly journals The Myc Transactivation Domain Promotes Global Phosphorylation of the RNA Polymerase II Carboxy-Terminal Domain Independently of Direct DNA Binding

2007 ◽  
Vol 27 (6) ◽  
pp. 2059-2073 ◽  
Author(s):  
Victoria H. Cowling ◽  
Michael D. Cole
Keyword(s):  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Initiation ◽  
Target Genes ◽  
Dependent Manner ◽  
Transactivation Domain ◽  
Pol Ii ◽  
Terminal Domain ◽  
Ctd Phosphorylation

ABSTRACT Myc is a transcription factor which is dependent on its DNA binding domain for transcriptional regulation of target genes. Here, we report the surprising finding that Myc mutants devoid of direct DNA binding activity and Myc target gene regulation can rescue a substantial fraction of the growth defect in myc −/− fibroblasts. Expression of the Myc transactivation domain alone induces a transcription-independent elevation of the RNA polymerase II (Pol II) C-terminal domain (CTD) kinases cyclin-dependent kinase 7 (CDK7) and CDK9 and a global increase in CTD phosphorylation. The Myc transactivation domain binds to the transcription initiation sites of these promoters and stimulates TFIIH binding in an MBII-dependent manner. Expression of the Myc transactivation domain increases CDK mRNA cap methylation, polysome loading, and the rate of translation. We find that some traditional Myc transcriptional target genes are also regulated by this Myc-driven translation mechanism. We propose that Myc transactivation domain-driven RNA Pol II CTD phosphorylation has broad effects on both transcription and mRNA metabolism.

scholarly journals Abstract P-18: Phosphorylation of RNA Polymerase II C-Terminal Domain Affects Transcript Elongation Through Chromatin

2021 ◽  
Vol 11 (Suppl_1) ◽  
pp. S19-S19
Author(s):  
Sohail Akhtar ◽  
Elena Kotova ◽  
Nadezhda Gerasimova ◽  
Vasily Studitsky
Keyword(s):  
Rna Polymerase ◽  
Chromatin Structure ◽  
Full Length ◽  
Pol Ii ◽  
Terminal Domain ◽  
Significant Difference ◽  
Transcript Elongation ◽  
Hyperphosphorylated Form ◽  
Ctd Phosphorylation

Background: Transcription is the central point of gene regulation where the efficient maintenance of chromatin structure during the passage of RNA polymerase (Pol II) is critical for cell survival and functioning. The phosphorylation of carboxy-terminal domain (CTD) of the large subunit (Rpb1) of Pol II plays a key role in transcription through chromatin providing the binding and dissociation of factors essential for the mRNA biogenesis. Although the regulatory effect of chromatin structure on multiple stages of transcription has been well established, the role of CTD phosphorylation itself has not been systematically addressed. Methods: The effect of differentially phosphorylated Pol II-CTD on transcript elongation through chromatin was studied using in vitro transcription system based on mononucleosomes precisely positioned on DNA. The unphosphorylated and hyperphosphorylated Pol II-CTD were obtained using yeast genetics as well as in vitro kinase or phosphatases. Transcription rate and positions of pausing were measured using authentic elongation complexes comprising Pol II having different CTD phosphorylation states. The quantitative analysis of the transcripts was conducted using denaturing PAGE. Results: We observed a significant difference in the transcription through chromatin depending on CTD phosphorylation level. Thus, experiments on transcription of nucleosomes with Pol II isoforms have shown that the hyperphosphorylated form more efficiently transcribes the nucleosome and leads to a faster accumulation of the full-length RNA product than the non-phosphorylated isoform of Pol II. The non-phosphorylated isoform of the enzyme is characterized by a stronger pause in the early nucleosomal region and a slower accumulation of the full-length RNA product. Conclusion: Hyperphosphorylated form more efficiently transcribes the nucleosome and leads to a faster accumulation of the full-length RNA product as compared with the non-phosphorylated isoform of Pol II. A preliminary model of the effect of Pol II hyperphosphorylation on nucleosomal DNA transcription is proposed.

scholarly journals CTD-dependent and - independent mechanisms govern co-transcriptional capping of Pol II transcripts

2018 ◽  
Author(s):  
Melvin Noe Gonzalez ◽  
Shigeo Sato ◽  
Chieri Tomomori-Sato ◽  
Joan W. Conaway ◽  
Ronald C. Conaway
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Pol Ii ◽  
Transcription System ◽  
Capping Enzyme ◽  
Dependent Processes ◽  
Ctd Phosphorylation

AbstractCo-transcriptional capping of RNA polymerase II (Pol II) transcripts by capping enzyme proceeds orders of magnitude more efficiently than capping of free RNA. Previous studies brought to light a role for the phosphorylated Pol II CTD in activation of co-transcriptional capping; however, CTD phosphorylation alone could not account for the observed magnitude of activation. Here, we exploit a defined Pol II transcription system that supports both CTD phosphorylation and robust activation of capping to dissect the mechanism of co-transcriptional capping. Taken together, our findings identify a novel CTD-independent, but Pol II-mediated, mechanism that functions in parallel with CTD-dependent processes to ensure optimal capping, and they support a “tethering” model for the mechanism of activation.

scholarly journals RNA polymerase II clustering through CTD phase separation

2018 ◽  
Author(s):  
M. Boehning ◽  
C. Dugast-Darzacq ◽  
M. Rankovic ◽  
A. S. Hansen ◽  
T. Yu ◽  
...  
Keyword(s):  
Phase Separation ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Initiation ◽  
Low Complexity ◽  
Initiation Factor ◽  
Published Data ◽  
Pol Ii ◽  
Intrinsically Disordered ◽  
Ctd Phosphorylation

The carboxy-terminal domain (CTD) of RNA polymerase (Pol) II is an intrinsically disordered low-complexity region that is critical for pre-mRNA transcription and processing. The CTD consists of hepta-amino acid repeats varying in number from 52 in humans to 26 in yeast. Here we report that human and yeast CTDs undergo cooperative liquid phase separation at increasing protein concentration, with the shorter yeast CTD forming less stable droplets. In human cells, truncation of the CTD to the length of the yeast CTD decreases Pol II clustering and chromatin association whereas CTD extension has the opposite effect. CTD droplets can incorporate intact Pol II and are dissolved by CTD phosphorylation with the transcription initiation factor IIH kinase CDK7. Together with published data, our results suggest that Pol II forms clusters/hubs at active genes through interactions between CTDs and with activators, and that CTD phosphorylation liberates Pol II enzymes from hubs for promoter escape and transcription elongation.

scholarly journals DSIF and RNA Polymerase II CTD Phosphorylation Coordinate the Recruitment of Rpd3S to Actively Transcribed Genes

PLoS Genetics ◽  
2010 ◽  
Vol 6 (10) ◽  
pp. e1001173 ◽  
Author(s):  
Simon Drouin ◽  
Louise Laramée ◽  
Pierre-Étienne Jacques ◽  
Audrey Forest ◽  
Maxime Bergeron ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Polymerase Ii Ctd ◽  
Ctd Phosphorylation
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