Sequence, structural and functional conservation among the human and fission yeast ELL and EAF transcription elongation factors

2021 ◽  
Author(s):  
Kumari Sweta ◽  
Preeti Dabas ◽  
Nimisha Sharma
Keyword(s):  
Fission Yeast ◽  
Transcription Elongation ◽  
Elongation Factors ◽  
Functional Conservation

CHAPTER 4. RNA Polymerase-associated Transcription Elongation Factors

2021 ◽  
pp. 72-99
Author(s):  
Shun-ichi Sekine ◽  
Tamami Uejima ◽  
Haruhiko Ehara
Keyword(s):  
Rna Polymerase ◽  
Transcription Elongation ◽  
Elongation Factors

scholarly journals The Rpb6 Subunit of Fission Yeast RNA Polymerase II Is a Contact Target of the Transcription Elongation Factor TFIIS

2000 ◽  
Vol 20 (4) ◽  
pp. 1263-1270 ◽  
Author(s):  
Akira Ishiguro ◽  
Yasuhisa Nogi ◽  
Koji Hisatake ◽  
Masami Muramatsu ◽  
Akira Ishihama
Keyword(s):  
Rna Polymerase ◽  
Fission Yeast ◽  
Rna Polymerase Ii ◽  
Transcription Elongation ◽  
Elongation Factor ◽  
Direct Interaction ◽  
Temperature Sensitive ◽  
Single Mutation ◽  
Transcription Elongation Factor ◽  
Essential Region

ABSTRACT The Rpb6 subunit of RNA polymerase II is one of the five subunits common to three forms of eukaryotic RNA polymerase. Deletion and truncation analyses of the rpb6 gene in the fission yeastSchizosaccharomyces pombe indicated that Rpb6, consisting of 142 amino acid residues, is an essential protein for cell viability, and the essential region is located in the C-terminal half between residues 61 and 139. After random mutagenesis, a total of 14 temperature-sensitive mutants were isolated, each carrying a single (or double in three cases and triple in one) mutation. Four mutants each carrying a single mutation in the essential region were sensitive to 6-azauracil (6AU), which inhibits transcription elongation by depleting the intracellular pool of GTP and UTP. Both 6AU sensitivity and temperature-sensitive phenotypes of these rpb6 mutants were suppressed by overexpression of TFIIS, a transcription elongation factor. In agreement with the genetic studies, the mutant RNA polymerases containing the mutant Rpb6 subunits showed reduced affinity for TFIIS, as measured by a pull-down assay of TFIIS-RNA polymerase II complexes using a fusion form of TFIIS with glutathioneS-transferase. Moreover, the direct interaction between TFIIS and RNA polymerase II was competed by the addition of Rpb6. Taken together, the results lead us to propose that Rpb6 plays a role in the interaction between RNA polymerase II and the transcription elongation factor TFIIS.

scholarly journals HIV-1 Tat and Host AFF4 Recruit Two Transcription Elongation Factors into a Bifunctional Complex for Coordinated Activation of HIV-1 Transcription

2010 ◽  
Vol 38 (3) ◽  
pp. 428-438 ◽  
Author(s):  
Nanhai He ◽  
Min Liu ◽  
Joanne Hsu ◽  
Yuhua Xue ◽  
Seemay Chou ◽  
...  
Keyword(s):  
Transcription Elongation ◽  
Elongation Factors ◽  
Hiv 1

scholarly journals The PAF Complex and Prf1/Rtf1 Delineate Distinct Cdk9-Dependent Pathways Regulating Transcription Elongation in Fission Yeast

PLoS Genetics ◽  
2013 ◽  
Vol 9 (12) ◽  
pp. e1004029 ◽  
Author(s):  
Jean Mbogning ◽  
Stephen Nagy ◽  
Viviane Pagé ◽  
Beate Schwer ◽  
Stewart Shuman ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Transcription Elongation ◽  
Paf Complex

scholarly journals Complementation of fission yeast kinesin-5/Cut7 with human Eg5 provides a versatile platform for screening of anti-cancer compounds

2021 ◽  
Author(s):  
Woosang Hwang ◽  
Takashi Toda ◽  
Masashi Yukawa
Keyword(s):  
Fission Yeast ◽  
Spindle Assembly ◽  
Cancer Drugs ◽  
Bipolar Spindle ◽  
Functional Conservation ◽  
Anti Cancer

Abstract Kinesin-5 family proteins are essential for bipolar spindle assembly to ensure mitotic fidelity. Here we demonstrate evolutionary functional conservation of kinesin-5 between human and fission yeast. Human Eg5 expressed in the nucleus replaces fission yeast counterpart Cut7. Intriguingly, Eg5 overproduction results in cytotoxicity. This phenotype provides a useful platform for the development of novel kinesin-5 inhibitors as anti-cancer drugs.

Structural insight into nucleosome transcription by RNA polymerase II with elongation factors

Science ◽  
2019 ◽  
Vol 363 (6428) ◽  
pp. 744-747 ◽  
Author(s):  
Haruhiko Ehara ◽  
Tomoya Kujirai ◽  
Yuka Fujino ◽  
Mikako Shirouzu ◽  
Hitoshi Kurumizaka ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Elongation ◽  
Chromosomal Dna ◽  
Elongation Factors ◽  
Cryo Electron Microscopy ◽  
Structural Insight ◽  
Insight Into

RNA polymerase II (RNAPII) transcribes chromosomal DNA that contains multiple nucleosomes. The nucleosome forms transcriptional barriers, and nucleosomal transcription requires several additional factors in vivo. We demonstrate that the transcription elongation factors Elf1 and Spt4/5 cooperatively lower the barriers and increase the RNAPII processivity in the nucleosome. The cryo–electron microscopy structures of the nucleosome-transcribing RNAPII elongation complexes (ECs) reveal that Elf1 and Spt4/5 reshape the EC downstream edge and intervene between RNAPII and the nucleosome. They facilitate RNAPII progression through superhelical location SHL(–1) by adjusting the nucleosome in favor of the forward progression. They suppress pausing at SHL(–5) by preventing the stable RNAPII-nucleosome interaction. Thus, the EC overcomes the nucleosomal barriers while providing a platform for various chromatin functions.

scholarly journals Nus transcription elongation factors and RNase III modulate small ribosome subunit biogenesis inEscherichia coli

2012 ◽  
Vol 87 (2) ◽  
pp. 382-393 ◽  
Author(s):  
Mikhail Bubunenko ◽  
Donald L. Court ◽  
Abdalla Al Refaii ◽  
Shivalika Saxena ◽  
Alexey Korepanov ◽  
...  
Keyword(s):  
Transcription Elongation ◽  
Inescherichia Coli ◽  
Elongation Factors ◽  
Rnase Iii
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