Control of Transcriptionin Bacillus brevis by Small Molecules

Paulus, Henry; Sarkar, Nirmal Kumar

doi:10.1007/978-1-4613-4529-9_3

Control of Transcription 1974

DOI: 10.1007/978-1-4613-4529-9_3

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Control of Transcriptionin Bacillus brevis by Small Molecules

Henry Paulus

Nirmal Kumar Sarkar

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1983

1996

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Cited by 4 publications

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“…Yet at the same time, an indication that bacterial RNA polyadenylation is physiologically significant emerged from studies on RNA synthesis in permeabilized cells of Bacillus breuis, where the degradation of newly synthesized RNA is primarily due to the action of a 3'-exonuclease that is inhibited by guanosine 3',5'-monophosphate (Paulus & Sarkar, 1974;Sarkar & Paulus, 1975). This 3'-exonuclease acts much more slowly on poly(A) than on other polynucleotides, suggesting that the stability of bacterial mRNA might be modulated by polyadenylation.…”

mentioning

confidence: 99%

Polyadenylation of mRNA in bacteria

Sarkar

1996

Microbiology

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mentioning

confidence: 99%

Polyadenylation of mRNA in bacteria

Sarkar

1996

Microbiology

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Biotin analogs activate guanylate cyclase

1984

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The sulfur atom in the vitamin biotin has previously been suggested to be essential in biotin's mechanism of action. In a series of investigations on structure-function relationships with biotin analogs not containing the sulfur atom, the biotin analogs, azabiotin, bisnorazabiotin, carbobiotin and isoazabiotin enhanced guanylate cyclase, an enzyme that has recently been demonstrated to be activated by biotin. These analogs increased guanylate cyclase activity two-fold in liver, cerebellum, heart, kidney and colon at 1 microM concentrations. The ED50 for stimulation of guanulate cyclase activity occurred at 0.1 microM for each of the biotin analogs. These data indicate that the sulfur atom is not essential in biotin's activation of guanylate cyclase since these analogs do not contain the sulfur atom. Studies on the ring structure of biotin revealed that even compounds with a single 5-membered ring (2-imidazolidone) could augment guanylate cyclase activity. The guanylate cyclase co-factor manganese was not essential for the enhancement of guanylate cyclase by these agents but a maximal activation of this enzyme by these analogs could not be obtained without manganese present.

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Cimetidine Partially Blocks Gastrin's Activation of Gastric Mucosal Guanylate Cyclase

Vesely

Meiners

1983

Endocrinology

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The objective of the present investigation was to determine if gastrin at physiological concentrations has part of its mechanism(s) of action through stimulation of guanylate cyclase (EC 4.6.1.2). Human gastrin (I), pentagastrin, tetragastrin, and gastrin-related tetrapeptide all increased cyclic GMP levels and guanylate cyclase activity in rat gastric mucosa, whole stomach, and duodenum. Maximal stimulation was seen at 1 microM with all of the above. There was no further enhancement of guanylate cyclase with increasing the concentration to the millimolar range. The ED50 for human gastrin and pentagastrin was 0.01 microM, whereas the ED50 was 0.1 microM for tetragastrin and the tetrapeptide. No enhancement of guanylate cyclase activity was seen with decreasing the concentration to 1 nM of the respective gastrins. Cimetidine utilized at 1 microM or 1 mM concentrations partially blocked the augmentation by gastrin suggesting that part of this enhancement was through the histamine 2 receptor which has been shown to be important in pentagastrin-stimulated gastric acid release. Since the block was only partial these data would also indicate that some part of gastrin's activation of this enzyme is not mediated through the histamine 2 receptor.

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Control of Transcriptionin Bacillus brevis by Small Molecules

Cited by 4 publications

References 8 publications

Polyadenylation of mRNA in bacteria

Polyadenylation of mRNA in bacteria

Biotin analogs activate guanylate cyclase

Cimetidine Partially Blocks Gastrin's Activation of Gastric Mucosal Guanylate Cyclase

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