scholarly journals The Length, Phosphorylation State, and Primary Structure of the RNA Polymerase II Carboxyl-terminal Domain Dictate Interactions with mRNA Capping Enzymes

2001 ◽  
Vol 276 (30) ◽  
pp. 28075-28082 ◽  
Author(s):  
Yi Pei ◽  
Stéphane Hausmann ◽  
C. Kiong Ho ◽  
Beate Schwer ◽  
Stewart Shuman
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Primary Structure ◽  
Phosphorylation State ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Mrna Capping ◽  
Carboxyl Terminal ◽  
Capping Enzymes

scholarly journals The Guanylyltransferase Domain of Mammalian mRNA Capping Enzyme Binds to the Phosphorylated Carboxyl-terminal Domain of RNA Polymerase II

1998 ◽  
Vol 273 (16) ◽  
pp. 9577-9585 ◽  
Author(s):  
C. Kiong Ho ◽  
Verl Sriskanda ◽  
Susan McCracken ◽  
David Bentley ◽  
Beate Schwer ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Mrna Capping ◽  
Capping Enzyme ◽  
Carboxyl Terminal

scholarly journals Separable Functions of the Fission Yeast Spt5 Carboxyl-Terminal Domain (CTD) in Capping Enzyme Binding and Transcription Elongation Overlap with Those of the RNA Polymerase II CTD

2010 ◽  
Vol 30 (10) ◽  
pp. 2353-2364 ◽  
Author(s):  
Susanne Schneider ◽  
Yi Pei ◽  
Stewart Shuman ◽  
Beate Schwer
Keyword(s):  
Rna Polymerase ◽  
Fission Yeast ◽  
Rna Polymerase Ii ◽  
Transcription Elongation ◽  
Pol Ii ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Capping Enzyme ◽  
Carboxyl Terminal ◽  
Capping Enzymes

ABSTRACT An interaction network connecting mRNA capping enzymes, the RNA polymerase II (Pol II) carboxyl-terminal domain (CTD), elongation factor Spt5, and the Cdk7 and Cdk9 protein kinases is thought to comprise a transcription elongation checkpoint. A crux of this network is Spt5, which regulates early transcription elongation and has an imputed role in pre-mRNA processing via its physical association with capping enzymes. Schizosaccharomyces pombe Spt5 has a distinctive CTD composed of tandem nonapeptide repeats of the consensus sequence 1TPAWNSGSK9. The Spt5 CTD binds the capping enzymes and is a substrate for threonine phosphorylation by the Cdk9 kinase. Here we report that deletion of the S. pombe Spt5 CTD results in slow growth and aberrant cell morphology. The severity of the spt5-ΔCTD phenotype is exacerbated by truncation of the Pol II CTD and ameliorated by overexpression of the capping enzymes RNA triphosphatase and RNA guanylyltransferase. These results suggest that the Spt5 and Pol II CTDs play functionally overlapping roles in capping enzyme recruitment. We probed structure-activity relations of the Spt5 CTD by alanine scanning of the consensus nonapeptide. The T1A change abolished CTD phosphorylation by Cdk9 but did not affect CTD binding to the capping enzymes. The T1A and P2A mutations elicited cold-sensitive (cs) and temperature-sensitive (ts) growth defects and conferred sensitivity to growth inhibition by 6-azauracil that was exacerbated by partial truncations of the Pol II CTD. The T1A phenotypes were rescued by a phosphomimetic T1E change but not by capping enzyme overexpression. These results imply a positive role for Spt5 CTD phosphorylation in Pol Il transcription elongation in fission yeast, distinct from its capping enzyme interactions. Viability of yeast cells bearing both Spt5 CTD T1A and Pol II CTD S2A mutations heralds that the Cdk9 kinase has an essential target other than Spt5 and Pol II CTD-Ser2.

scholarly journals Rsp5 WW Domains Interact Directly with the Carboxyl-terminal Domain of RNA Polymerase II

2000 ◽  
Vol 275 (27) ◽  
pp. 20562-20571 ◽  
Author(s):  
Alex Chang ◽  
Sonny Cheang ◽  
Xavier Espanel ◽  
Marius Sudol
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Ww Domains ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Carboxyl Terminal

scholarly journals JMJD5 couples with CDK9 to release the paused RNA polymerase II

2020 ◽  
Vol 117 (33) ◽  
pp. 19888-19895
Author(s):  
Haolin Liu ◽  
Srinivas Ramachandran ◽  
Nova Fong ◽  
Tzu Phang ◽  
Schuyler Lee ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Elongation Factor ◽  
Pol Ii ◽  
Transcription Start Sites ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Pol Ii Pausing ◽  
Carboxyl Terminal ◽  
Heptad Repeats

More than 30% of genes in higher eukaryotes are regulated by RNA polymerase II (Pol II) promoter proximal pausing. Pausing is released by the positive transcription elongation factor complex (P-TEFb). However, the exact mechanism by which this occurs and whether phosphorylation of the carboxyl-terminal domain of Pol II is involved in the process remains unknown. We previously reported that JMJD5 could generate tailless nucleosomes at position +1 from transcription start sites (TSS), thus perhaps enable progression of Pol II. Here we find that knockout of JMJD5 leads to accumulation of nucleosomes at position +1. Absence of JMJD5 also results in loss of or lowered transcription of a large number of genes. Interestingly, we found that phosphorylation, by CDK9, of Ser2 within two neighboring heptad repeats in the carboxyl-terminal domain of Pol II, together with phosphorylation of Ser5 within the second repeat, HR-Ser2p (1, 2)-Ser5p (2) for short, allows Pol II to bind JMJD5 via engagement of the N-terminal domain of JMJD5. We suggest that these events bring JMJD5 near the nucleosome at position +1, thus allowing JMJD5 to clip histones on this nucleosome, a phenomenon that may contribute to release of Pol II pausing.

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