Nucleoside Triphosphate Levels in Streptomyces hydrogenans during Growth and Induction of 20β-Hydroxysteroid Dehydrogenase

1976 ◽  
Vol 31 (7-8) ◽  
pp. 486-487
Author(s):  
Joachim Betz ◽  
Lothar Träger
Keyword(s):  
Growth Medium ◽  
Hydroxysteroid Dehydrogenase ◽  
Purine Nucleoside ◽  
Nucleoside Triphosphate ◽  
Phase Growth ◽  
Nucleoside Triphosphates

Abstract Levels of the purine nucleoside triphosphates are de­ creasing towards the end of log phase growth of Streptomyces hydrogenans. Induction of 20β-hydroxysteroid dehy-drogenase by addition of 11β,21-dihydroxy-4,17 (20) -pregna-dien-3-one to the growth medium leads to a pronounced drop in purine nucleoside triphosphate levels with is irreversible in contrast to the initial loss and later accumulation of RNA.

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 semisynthetic organism engineered for the stable expansion of the genetic alphabet

2017 ◽  
Vol 114 (6) ◽  
pp. 1317-1322 ◽  
Author(s):  
Yorke Zhang ◽  
Brian M. Lamb ◽  
Aaron W. Feldman ◽  
Anne Xiaozhou Zhou ◽  
Thomas Lavergne ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Base Pair ◽  
Genetic Information ◽  
Information Storage ◽  
Nucleoside Triphosphate ◽  
Proof Of Concept ◽  
Sequence Context ◽  
Form Of Life ◽  
Nucleoside Triphosphates ◽  
Genetic Alphabet

All natural organisms store genetic information in a four-letter, two-base-pair genetic alphabet. The expansion of the genetic alphabet with two synthetic unnatural nucleotides that selectively pair to form an unnatural base pair (UBP) would increase the information storage potential of DNA, and semisynthetic organisms (SSOs) that stably harbor this expanded alphabet would thereby have the potential to store and retrieve increased information. Toward this goal, we previously reported thatEscherichia coligrown in the presence of the unnatural nucleoside triphosphates dNaMTP and d5SICSTP, and provided with the means to import them via expression of a plasmid-borne nucleoside triphosphate transporter, replicates DNA containing a single dNaM-d5SICS UBP. Although this represented an important proof-of-concept, the nascent SSO grew poorly and, more problematically, required growth under controlled conditions and even then was unable to indefinitely store the unnatural information, which is clearly a prerequisite for true semisynthetic life. Here, to fortify and vivify the nascent SSO, we engineered the transporter, used a more chemically optimized UBP, and harnessed the power of the bacterial immune response by using Cas9 to eliminate DNA that had lost the UBP. The optimized SSO grows robustly, constitutively imports the unnatural triphosphates, and is able to indefinitely retain multiple UBPs in virtually any sequence context. This SSO is thus a form of life that can stably store genetic information using a six-letter, three-base-pair alphabet.

scholarly journals Enzymatic Formation of an Artificial Base Pair Using a Modified Purine Nucleoside Triphosphate

2020 ◽  
Vol 15 (11) ◽  
pp. 2872-2884
Author(s):  
Marie Flamme ◽  
Pascal Röthlisberger ◽  
Fabienne Levi-Acobas ◽  
Mohit Chawla ◽  
Romina Oliva ◽  
...  
Keyword(s):  
Base Pair ◽  
Purine Nucleoside ◽  
Nucleoside Triphosphate ◽  
Enzymatic Formation

scholarly journals Changes in the Concentrations of Guanosine 5′-Diphosphate 3′-Diphosphate and the Initiating Nucleoside Triphosphate Account for Inhibition of rRNA Transcription in Fructose-1,6-Diphosphate Aldolase (fda) Mutants

2003 ◽  
Vol 185 (20) ◽  
pp. 6192-6194 ◽  
Author(s):  
David A. Schneider ◽  
Richard L. Gourse
Keyword(s):  
Glycolytic Enzyme ◽  
Rrna Synthesis ◽  
Nucleoside Triphosphate ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Lethal Mutations ◽  
Rrna Transcription ◽  
Mechanism Of Inhibition ◽  
Nucleoside Triphosphates ◽  
Standing Question

ABSTRACT Early screens for conditional lethal mutations that affected rRNA expression in Escherichia coli identified temperature-sensitive fda mutants (fda encodes the glycolytic enzyme fructose-1,6-diphosphate aldolase). It was shown that these fda(Ts) mutants were severely impaired in rRNA synthesis upon shift to the restrictive temperature, although the mechanism of inhibition was never determined. Here, we bring resolution to this long-standing question by showing that changes in the concentrations of guanosine 5′-diphosphate 3′-diphosphate and initiating nucleoside triphosphates can account for the previously observed effects of fda mutations on rRNA transcription.

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