Minimal Machinery of RNA Polymerase Holoenzyme Sufficient for Promoter Melting

Science ◽  
2004 ◽  
Vol 303 (5662) ◽  
pp. 1382-1384 ◽  
Author(s):  
B. A. Young
Keyword(s):  
Rna Polymerase ◽  
Promoter Melting ◽  
Rna Polymerase Holoenzyme

scholarly journals Utilization of variably spaced promoter-like elements by the bacterial RNA polymerase holoenzyme during early elongation

2010 ◽  
Vol 75 (3) ◽  
pp. 607-622 ◽  
Author(s):  
Pukhrambam Grihanjali Devi ◽  
Elizabeth A. Campbell ◽  
Seth A. Darst ◽  
Bryce E. Nickels
Keyword(s):  
Rna Polymerase ◽  
Bacterial Rna ◽  
Rna Polymerase Holoenzyme

scholarly journals Effect of disulfide and sulfhydryl reagents on abortive and productive elongation catalyzed by Escherichia coli RNA polymerase.

1994 ◽  
Vol 41 (4) ◽  
pp. 415-419
Author(s):  
M Radłowski ◽  
D Job
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Fold Increase ◽  
Sulfhydryl Reagents ◽  
Nitrobenzoic Acid ◽  
Steady State Kinetic ◽  
Transcription Complexes ◽  
The Stability ◽  
Rna Polymerase Holoenzyme ◽  
Productive Elongation

The effect of disulfide and sulfhydryl reagents on the rate of abortive and productive elongation has been studied using Escherichia coli RNA polymerase holoenzyme and poly[d(A-T)] as template. In the presence of UTP as a single substrate and UpA as a primer, the enzyme catalyzed efficiently the synthesis of the trinucleotide product UpApU. Incubation of RNA polymerase with 1 mM 2-mercaptoethanol resulted in a 5-fold increase of the rate of UpApU synthesis. In contrast, incubation of the enzyme with 1 mM 5,5'-dithio-bis(2-nitrobenzoic) acid resulted in a 6-fold decrease of the rate of abortive elongation. Determination of the steady state kinetic constants associated with UpApU synthesis disclosed that the disulfide and sulfhydryl reagents mainly affected the rate of UpApU release from the ternary transcription complexes and therefore influenced the stability of such complexes.

scholarly journals Cryo-EM structures reveal transcription initiation steps by yeast mitochondrial RNA polymerase

2020 ◽  
Author(s):  
Brent De Wijngaert ◽  
Shemaila Sultana ◽  
Chhaya Dharia ◽  
Hans Vanbuel ◽  
Jiayu Shen ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Large Scale ◽  
Rna Synthesis ◽  
Mitochondrial Rna ◽  
Initiation Complex ◽  
Mitochondrial Rna Polymerase ◽  
Catalytically Active ◽  
Promoter Melting ◽  
Antiviral Nucleosides

Cryo-EM structures of transcription pre-initiation complex (PIC) and initiation complex (IC) of yeast mitochondrial RNA polymerase show fully resolved transcription bubbles and explain promoter melting, template alignment, DNA scrunching, transition into elongation, and abortive synthesis. Promoter melting initiates in PIC with MTF1 trapping the −4 to −2 non-template (NT) bases in its NT-groove. Transition to IC is marked by a large-scale movement that aligns the template with RNA at the active site. RNA synthesis scrunches the NT strand into an NT-loop, which interacts with centrally positioned MTF1 C-tail. Steric clashes of the C-tail with RNA:DNA and NT-loop, and dynamic scrunching-unscrunching of DNA explain abortive synthesis and transition into elongation. Capturing the catalytically active IC-state with UTPαS poised for incorporation enables modeling toxicity of antiviral nucleosides/nucleotides.

Purification, crystallization and initial crystallographic analysis of RNA polymerase holoenzyme fromThermus thermophilus

2002 ◽  
Vol 58 (9) ◽  
pp. 1497-1500 ◽  
Author(s):  
Marina N. Vassylyeva ◽  
Jookyung Lee ◽  
Shun-ichi Sekine ◽  
Oleg Laptenko ◽  
Seiki Kuramitsu ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Crystallographic Analysis ◽  
Rna Polymerase Holoenzyme
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