scholarly journals Intrasubunit nucleotide binding in ribonucleic acid polymerase

1978 ◽  
Vol 175 (1) ◽  
pp. 189-192 ◽  
Author(s):  
A D B Malcolm ◽  
J R Moffatt
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Ribonucleic Acid ◽  
Periodate Oxidation ◽  
Nucleotide Binding ◽  
Alpha Subunit ◽  
Nucleoside Triphosphate ◽  
Competitive Inhibitors ◽  
Nucleoside Triphosphates ◽  
Derivatives Of

1. Periodate oxidation of the ribose ring was used to synthesize derivatives of nucleoside triphosphates. 2. These oxidized nucleoside triphosphates. 2. These oxidized nucleoside triphosphates are competitive inhibitors of RNA polymerase. 3. On incubation, together with NaBH4, these oxidized labelled nucleotides are covalently bound to Escherichia coli RNA polymerase. 4. Nucleoside triphosphate substrates decrease the extent of labelling. 5. A lysine residue in an alpha-subunit is labelled. 6. The significance of these results in relation to the location of the nucleotide-binding site is discussed.

scholarly journals Nucleic acid enzymology of extremely halophilic bacteria. Halobacterium cutirubrum deoxyribonucleic acid-dependent ribonucleic acid polymerase

1971 ◽  
Vol 121 (4) ◽  
pp. 621-627 ◽  
Author(s):  
B. Gregory Louis ◽  
P. S. Fitt
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Rna Polymerase ◽  
Deoxyribonucleic Acid ◽  
Halophilic Bacteria ◽  
Nucleoside Triphosphate ◽  
Extreme Halophile ◽  
Univalent Cations ◽  
Absolute Requirement ◽  
Nucleoside Triphosphates

1. DNA-dependent RNA polymerase was purified 150-fold from crude extracts of the extreme halophile Halobacterium cutirubrum. 2. The enzyme requires the presence of native DNA and all four nucleoside triphosphates to incorporate 14C-labelled nucleoside triphosphate into an acid-insoluble ribonuclease-sensitive product. 3. It has an absolute requirement for both Mn2+ and Mg2+. 4. The polymerase requires a high salt concentration for stability, but is markedly inhibited by univalent cations. 5. Its molecular weight is very low compared with that of Escherichia coli RNA polymerase.

scholarly journals A procedure for the rapid purification of Escherichia coli deoxyribonucleic acid-dependent ribonucleic acid polymerase (Short Communication)

1973 ◽  
Vol 133 (1) ◽  
pp. 201-203 ◽  
Author(s):  
Peter Humphries ◽  
David J. McConnell ◽  
Robert L. Gordon
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Ribonucleic Acid ◽  
Deoxyribonucleic Acid ◽  
Short Communication ◽  
Gel Filtration ◽  
High Salt ◽  
Rapid Procedure ◽  
Complete Purification ◽  
Rapid Purification

A rapid procedure involving DNA–cellulose chromatography followed either by sedimentation in a high-salt glycerol gradient or by gel filtration is described for the complete purification of Escherichia coli DNA-dependent RNA polymerase.

scholarly journals Derivatives of guanosine triphosphate-photoreactive substrates of escherichia coli RNA polymerase

FEBS Letters ◽  
1980 ◽  
Vol 112 (2) ◽  
pp. 296-298 ◽  
Author(s):  
E.D. Sverdlov ◽  
S.A. Tsarev ◽  
N.F. Kuznetsova
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Guanosine Triphosphate ◽  
Derivatives Of

Action of Trifluralin on Chromatin Activity in Corn and Soybean

Weed Science ◽  
1972 ◽  
Vol 20 (4) ◽  
pp. 364-366 ◽  
Author(s):  
Donald Penner ◽  
Roy W. Early
Keyword(s):  
Escherichia Coli ◽  
Zea Mays ◽  
Glycine Max ◽  
Rna Polymerase ◽  
Melting Temperature ◽  
Ribonucleic Acid ◽  
Rna Synthesis ◽  
Subsequent Reduction

Trifluralin (α,α,α-trifluoro-2,6-dinitro-N,N-dipropyl-p-toluidine) at 10−5M applied to etiolated corn(Zea maysL. ‘Michigan 500′) seedlings 6 or 12 hr before the isolation of chromatin from the roots markedly reduced ribonucleic acid (RNA) synthesis supported by the chromatin. The addition ofEscherichia coliRNA polymerase failed to overcome the inhibition. Trifluralin increased the melting temperature of the chromatin. The presence of trifluralin during the isolation and reaction procedure inhibited RNA synthesis indicating possible trifluralin binding to the chromatin with subsequent reduction of template availability for transcription. Trifluralin did not inhibit chromatin activity in soybean [Glycine max(L.) Merr. ‘Hark’] seedlings.

scholarly journals Trigger loop folding determines transcription rate of Escherichia coli’s RNA polymerase

2014 ◽  
Vol 112 (3) ◽  
pp. 743-748 ◽  
Author(s):  
Yara X. Mejia ◽  
Evgeny Nudler ◽  
Carlos Bustamante
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Single Molecule ◽  
Conformational Changes ◽  
Elongation Rate ◽  
Nucleoside Triphosphate ◽  
Transcription Rate ◽  
Nucleotide Analogs ◽  
Catalytic Center ◽  
Trigger Loop

Two components of the RNA polymerase (RNAP) catalytic center, the bridge helix and the trigger loop (TL), have been linked with changes in elongation rate and pausing. Here, single molecule experiments with the WT and two TL-tip mutants of the Escherichia coli enzyme reveal that tip mutations modulate RNAP’s pause-free velocity, identifying TL conformational changes as one of two rate-determining steps in elongation. Consistent with this observation, we find a direct correlation between helix propensity of the modified amino acid and pause-free velocity. Moreover, nucleotide analogs affect transcription rate, suggesting that their binding energy also influences TL folding. A kinetic model in which elongation occurs in two steps, TL folding on nucleoside triphosphate (NTP) binding followed by NTP incorporation/pyrophosphate release, quantitatively accounts for these results. The TL plays no role in pause recovery remaining unfolded during a pause. This model suggests a finely tuned mechanism that balances transcription speed and fidelity.

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