scholarly journals A Novel Assay for RNA Polymerase I Transcription Elongation Sheds Light on the Evolutionary Divergence of Eukaryotic RNA Polymerases

Biochemistry ◽  
2019 ◽  
Vol 58 (16) ◽  
pp. 2116-2124 ◽  
Author(s):  
Catherine E. Scull ◽  
Zachariah M. Ingram ◽  
Aaron L. Lucius ◽  
David A. Schneider
Keyword(s):  
Rna Polymerase ◽  
Transcription Elongation ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Evolutionary Divergence ◽  
Polymerase I

scholarly journals Small-Molecule Targeting of RNA Polymerase I Activates a Conserved Transcription Elongation Checkpoint

Cell Reports ◽  
2018 ◽  
Vol 23 (2) ◽  
pp. 404-414 ◽  
Author(s):  
Ting Wei ◽  
Saman M. Najmi ◽  
Hester Liu ◽  
Karita Peltonen ◽  
Alena Kucerova ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Small Molecule ◽  
Transcription Elongation ◽  
Rna Polymerase I ◽  
Polymerase I

Inactivation of rat liver RNA polymerases I and II and yeast RNA polymerase I by pyridoxal 5'-phosphate. Evidence for the participation of lysyl residues at the active site

Biochemistry ◽  
1975 ◽  
Vol 14 (22) ◽  
pp. 4907-4911 ◽  
Author(s):  
Joseph Martial ◽  
Josefina Zaldivar ◽  
Paulina Bull ◽  
Alejandro Venegas ◽  
Pablo Valenzuela
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Active Site ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Polymerase I

scholarly journals Histone Acetyltransferase and Protein Kinase Activities Copurify with a Putative Xenopus RNA Polymerase I Holoenzyme Self-Sufficient for Promoter-Dependent Transcription

1999 ◽  
Vol 19 (1) ◽  
pp. 796-806 ◽  
Author(s):  
Annie-Claude Albert ◽  
Michael Denton ◽  
Milko Kermekchiev ◽  
Craig S. Pikaard
Keyword(s):  
Rna Polymerase ◽  
Histone Acetyltransferase ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Large Mass ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Pol I ◽  
Coomassie Blue ◽  
Polymerase I

ABSTRACT Mounting evidence suggests that eukaryotic RNA polymerases preassociate with multiple transcription factors in the absence of DNA, forming RNA polymerase holoenzyme complexes. We have purified an apparent RNA polymerase I (Pol I) holoenzyme from Xenopus laevis cells by sequential chromatography on five columns: DEAE-Sepharose, Biorex 70, Sephacryl S300, Mono Q, and DNA-cellulose. Single fractions from every column programmed accurate promoter-dependent transcription. Upon gel filtration chromatography, the Pol I holoenzyme elutes at a position overlapping the peak of Blue Dextran, suggesting a molecular mass in the range of ∼2 MDa. Consistent with its large mass, Coomassie blue-stained sodium dodecyl sulfate-polyacrylamide gels reveal approximately 55 proteins in fractions purified to near homogeneity. Western blotting shows that TATA-binding protein precisely copurifies with holoenzyme activity, whereas the abundant Pol I transactivator upstream binding factor does not. Also copurifying with the holoenzyme are casein kinase II and a histone acetyltransferase activity with a substrate preference for histone H3. These results extend to Pol I the suggestion that signal transduction and chromatin-modifying activities are associated with eukaryotic RNA polymerases.

scholarly journals Direct Characterization of Transcription Elongation by RNA Polymerase I

PLoS ONE ◽  
2016 ◽  
Vol 11 (7) ◽  
pp. e0159527 ◽  
Author(s):  
Suleyman Ucuncuoglu ◽  
Krysta L. Engel ◽  
Prashant K. Purohit ◽  
David D. Dunlap ◽  
David A. Schneider ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Transcription Elongation ◽  
Rna Polymerase I ◽  
Polymerase I
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