scholarly journals The Drosophila trithorax group protein Kismet facilitates an early step in transcriptional elongation by RNA Polymerase II

Development ◽  
2005 ◽  
Vol 132 (7) ◽  
pp. 1623-1635 ◽  
Author(s):  
S. Srinivasan
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Elongation ◽  
Early Step ◽  
Trithorax Group ◽  
Group Protein

Identification of rpo30, a vaccinia virus RNA polymerase gene with structural similarity to a eucaryotic transcription elongation factor

1990 ◽  
Vol 10 (10) ◽  
pp. 5433-5441
Author(s):  
B Y Ahn ◽  
P D Gershon ◽  
E V Jones ◽  
B Moss
Keyword(s):  
Rna Polymerase ◽  
Vaccinia Virus ◽  
Rna Polymerase Ii ◽  
Elongation Factor ◽  
Viral Rna ◽  
In Vitro Translation ◽  
Virus Protein ◽  
Transcriptional Elongation

Eucaryotic transcription factors that stimulate RNA polymerase II by increasing the efficiency of elongation of specifically or randomly initiated RNA chains have been isolated and characterized. We have identified a 30-kilodalton (kDa) vaccinia virus-encoded protein with apparent homology to SII, a 34-kDa mammalian transcriptional elongation factor. In addition to amino acid sequence similarities, both proteins contain C-terminal putative zinc finger domains. Identification of the gene, rpo30, encoding the vaccinia virus protein was achieved by using antibody to the purified viral RNA polymerase for immunoprecipitation of the in vitro translation products of in vivo-synthesized early mRNA selected by hybridization to cloned DNA fragments of the viral genome. Western immunoblot analysis using antiserum made to the vaccinia rpo30 protein expressed in bacteria indicated that the 30-kDa protein remains associated with highly purified viral RNA polymerase. Thus, the vaccinia virus protein, unlike its eucaryotic homolog, is an integral RNA polymerase subunit rather than a readily separable transcription factor. Further studies showed that the expression of rpo30 is regulated by dual early and later promoters.

scholarly journals Mechanism and regulation of transcriptional elongation by RNA polymerase II

1999 ◽  
Vol 11 (3) ◽  
pp. 342-346 ◽  
Author(s):  
Daniel Reines ◽  
Ronald C Conaway ◽  
Joan Weliky Conaway
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Elongation

scholarly journals GSK-3 is an RNA polymerase II phospho-CTD kinase

2020 ◽  
Vol 48 (11) ◽  
pp. 6068-6080 ◽  
Author(s):  
Nicolás Nieto Moreno ◽  
Florencia Villafañez ◽  
Luciana E Giono ◽  
Carmen Cuenca ◽  
Gastón Soria ◽  
...  
Keyword(s):  
Dna Damage ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Glycogen Synthase ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Transcriptional Elongation ◽  
Induced Apoptosis ◽  
Carboxy Terminal

Abstract We have previously found that UV-induced DNA damage causes hyperphosphorylation of the carboxy terminal domain (CTD) of RNA polymerase II (RNAPII), inhibition of transcriptional elongation and changes in alternative splicing (AS) due to kinetic coupling between transcription and splicing. In an unbiased search for protein kinases involved in the AS response to DNA damage, we have identified glycogen synthase kinase 3 (GSK-3) as an unforeseen participant. Unlike Cdk9 inhibition, GSK-3 inhibition only prevents CTD hyperphosphorylation triggered by UV but not basal phosphorylation. This effect is not due to differential degradation of the phospho-CTD isoforms and can be reproduced, at the AS level, by overexpression of a kinase-dead GSK-3 dominant negative mutant. GSK-3 inhibition abrogates both the reduction in RNAPII elongation and changes in AS elicited by UV. We show that GSK-3 phosphorylates the CTD in vitro, but preferentially when the substrate is previously phosphorylated, consistently with the requirement of a priming phosphorylation reported for GSK-3 efficacy. In line with a role for GSK-3 in the response to DNA damage, GSK-3 inhibition prevents UV-induced apoptosis. In summary, we uncover a novel role for a widely studied kinase in key steps of eukaryotic transcription and pre-mRNA processing.

The Transcriptional Intermediary Factor TIF1γ Controls Erythroid Cell Fate by Specifically Regulating Transcriptional Elongation.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 254-254
Author(s):  
Xiaoying Bai ◽  
Joseph Lee ◽  
Jocelyn LeBlanc ◽  
Anna Sessa ◽  
Zhongan Yang ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Cell Fate ◽  
Erythroid Cell ◽  
Transcriptional Elongation ◽  
Pol Ii ◽  
Physical Interactions ◽  
Paf1 Complex

Abstract Abstract 254 Vertebrate erythropoiesis is regulated by cell-specific transcription factors, RNA polymerase-associated basal machinery and chromatin remodeling factors. One critical chromatin factor is the transcriptional intermediary factor TIF1γ. Loss of TIF1γfunction in zebrafish mutant moonshine causes a profound anemia during embryogenesis, associated with a progressive decrease in expression of most erythroid mRNAs such as GATA1 and globin. TIF1γdeficiency has also been linked to TGF-βsignaling, although the in vivo mechanism for the anemia remains unclear. In an effort to find genes that interact with TIF1γ, we undertook a genetic suppressor screen in which we sought mutations in another gene that would restore blood to normal levels in the background of moonshine deficiency. Few suppressor screens have been done in vertebrate genetic models, and the haploid genetics of zebrafish was a great advantage for this screen. After screening 800 families of fish, two suppressor mutants, “eclipse” and “sunrise”, were found that could greatly rescue the erythroid defects in moonshine. The deficient gene in sunrise has been mapped to the locus of cdc73 (also known as parafibromin/HRPT2), a subunit of the PAF1 complex known to regulate RNA polymerase II (Pol II) elongation and chromatin modification. Furthermore, we have found that knocking down other subunits in the PAF1 complex also rescued the blood defect in moonshine, suggesting that PAF1 as a complex antagonizes TIF1γfunction during erythropoiesis. In yeast, PAF1 has been shown to physically or genetically interact with other elongation factors including DSIF, FACT and p-TEFb. We have found that knocking down DSIF, which is known to induce Pol II pausing during early elongation, also rescues moonshine. FACT and p-TEFb are both known to counteract DSIF to release Pol II from pausing, and knocking down FACT and p-TEFb caused the zebrafish to develop anemia. This strongly suggests that the erythroid defects in TIF1γdeficiency is caused by attenuated Pol II elongation. In an effort to understand the cell-specific phenotype of TIF1γdeficiency, we introduced a FLAG tagged TIF1γinto K562 erythroleukemia cells to pull down interacting proteins. Physical interactions were found among TIF1γ, FACT, p-TEFb and surprisingly the SCL hematopoietic transcription complex. The interaction with the SCL complex provides a cell-specific control over transcriptional elongation. The physical interactions, taken together with the genetic data, suggest a novel mechanism regulating erythropoiesis. TIF1γphysically and functionally links blood-specific transcription factors like SCL to Pol II-associated elongation machinery to regulate blood cell fate. In light of the recent discoveries of widespread Pol II stalling in the promoter proximal region in metazoan genomes, we speculate that similar mechanisms will regulate cell fates in other blood lineages as well as non-blood tissues. Disclosures: Zon: FATE Inc: Consultancy, Equity Ownership, Membership on an entity's Board of Directors or advisory committees; Stemgent: Consultancy.

scholarly journals Domains in the SPT5 Protein That Modulate Its Transcriptional Regulatory Properties

2000 ◽  
Vol 20 (9) ◽  
pp. 2970-2983 ◽  
Author(s):  
Dmitri Ivanov ◽  
Youn Tae Kwak ◽  
Jun Guo ◽  
Richard B. Gaynor
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Repression ◽  
Transcriptional Elongation ◽  
Tat Protein ◽  
C Terminus ◽  
Heptad Repeats ◽  
And Function ◽  
Hiv 1

ABSTRACT SPT5 and its binding partner SPT4 regulate transcriptional elongation by RNA polymerase II. SPT4 and SPT5 are involved in both 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole (DRB)-mediated transcriptional inhibition and the activation of transcriptional elongation by the human immunodeficiency virus type 1 (HIV-1) Tat protein. Recent data suggest that P-TEFb, which is composed of CDK9 and cyclin T1, is also critical in regulating transcriptional elongation by SPT4 and SPT5. In this study, we analyze the domains of SPT5 that regulate transcriptional elongation in the presence of either DRB or the HIV-1 Tat protein. We demonstrate that SPT5 domains that bind SPT4 and RNA polymerase II, in addition to a region in the C terminus of SPT5 that contains multiple heptad repeats and is designated CTR1, are critical for in vitro transcriptional repression by DRB and activation by the Tat protein. Furthermore, the SPT5 CTR1 domain is a substrate for P-TEFb phosphorylation. These results suggest that C-terminal repeats in SPT5, like those in the RNA polymerase II C-terminal domain, are sites for P-TEFb phosphorylation and function in modulating its transcriptional elongation properties.

scholarly journals Critical Role of Transcript Cleavage in Arabidopsis RNA Polymerase II Transcriptional Elongation

2020 ◽  
Vol 32 (5) ◽  
pp. 1449-1463 ◽  
Author(s):  
Wojciech Antosz ◽  
Jules Deforges ◽  
Kevin Begcy ◽  
Astrid Bruckmann ◽  
Yves Poirier ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Critical Role ◽  
Transcriptional Elongation ◽  
Transcript Cleavage
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