scholarly journals Cleavage/polyadenylation factor IA associates with the carboxyl-terminal domain of RNA polymerase II in Saccharomyces cerevisiae

2001 ◽  
Vol 98 (2) ◽  
pp. 445-450 ◽  
Author(s):  
D. Barilla ◽  
B. A. Lee ◽  
N. J. Proudfoot
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Carboxyl Terminal ◽  
Polyadenylation Factor

scholarly journals SSN genes that affect transcriptional repression in Saccharomyces cerevisiae encode SIN4, ROX3, and SRB proteins associated with RNA polymerase II.

1996 ◽  
Vol 16 (1) ◽  
pp. 115-120 ◽  
Author(s):  
W Song ◽  
I Treich ◽  
N Qian ◽  
S Kuchin ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Activation ◽  
Transcriptional Repression ◽  
Cyclin Dependent Kinase ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Carboxyl Terminal ◽  
Insight Into

The RNA polymerase II of Saccharomyces cerevisiae exists in holoenzyme forms containing a complex, known as the mediator, associated with the carboxyl-terminal domain. The mediator includes several SRB proteins and is required for transcriptional activation. Previous work showed that a cyclin-dependent kinase-cyclin pair encoded by SSN3 and SSN8, two members of the SSN suppressor family, are identical to two SRB proteins in the mediator. Here we have identified the remaining SSN genes by cloning and genetic analysis. SSN2 and SSN5 are identical to SRB9 and SRB8, respectively, which encode additional components of the mediator. Genetic evidence implicates the SSN genes in transcriptional repression. Thus, these identities provide genetic insight into mediator and carboxyl-terminal domain function, strongly suggesting a role in mediating transcriptional repression as well as activation. We also show that SSN4 and SSN7 are the same as SIN4 and ROX3, respectively, raising the possibility that these genes also encode mediator proteins.

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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