Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase

Zamecnik, Paul G.; Stephenson, Mary L.; Janeway, Claude M.; Randerath, Kurt

doi:10.1016/0006-291x(66)90415-3

Cited by 266 publications

(126 citation statements)

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“…It has been shown in vitro that glycyl adenylate intermediates which are bound to glycyl-tRNA synthetase (Led et al 1983), or some other aminoacyl-tRNA synthetases (Zamecnik et al 1966) donate AMP to ATP, yielding Ap4A. However, the existence of such reactions in vivo has not been demonstrated; neither aminoacyl-tRNA synthetase mutations, inhibitory treatments of aminoacylation, nor structural mutations of tRNA are known to produce Ap4A in vivo (Bochner et al 1984).…”

Section: Discussionmentioning

confidence: 99%

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Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

et al. 1997

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Section: Discussionmentioning

confidence: 99%

“…The apaH encodes the diadenosine-tetraphosphate (Ap4A) hydrolase (Mechulam et al 1985) and Ap4A is synthesized in vitro by certain aminoacyl-tRNA synthetases (Zamecnik et al 1966). Complementation analysis showed that the plasmid encoding apaH þ partially complemented cfcA11 (Table 3).…”

Section: Cellular Level Of Ap4a In Both Cfca11 and Cfcb1 Is Highmentioning

confidence: 99%

Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

et al. 1997

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“…Scientists, when investigating the reaction between aminoacids and their corresponding tRNAs during the protein synthesis process discovered the presence of some diadenosine polyphosphates Zamecnik et al, 1966). Over the following years, most of the efforts were dedicated to describing their structural and chemical properties, mainly by spectrometric methods (Bush and Tinoco, 1967;Cheng, 1968;Warshaw and Tinoco, 1965).…”

Section: Dinucleoside Polyphosphates: Structure and Featuresmentioning

confidence: 99%

The role of dinucleoside polyphosphates on the ocular surface and other eye structures

Carracedo

Crooke

Guzmán-Aránguez

et al. 2016

Progress in Retinal and Eye Research

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a b s t r a c tDinucleoside polyphosphates comprises a group of dinucleotides formed by two nucleosides linked by a variable number of phosphates, abbreviated NpnN (where n represents the number of phosphates). These compounds are naturally occurring substances present in tears, aqueous humour and in the retina. As the consequence of their presence, these dinucleotides contribute to many ocular physiological processes. On the ocular surface, dinucleoside polyphosphates can stimulate tear secretion, mucin release from goblet cells and they help epithelial wound healing by accelerating cell migration rate. These dinucleotides can also stimulate the presence of proteins known to protect the ocular surface against microorganisms, such as lysozyme and lactoferrin. One of the latest discoveries is the ability of some dinucleotides to facilitate the paracellular way on the cornea, therefore allowing the delivery of compounds, such as antiglaucomatous ones, more easily within the eye. The compound Ap 4 A has been described being abnormally elevated in patient's tears suffering of dry eye, Sjogren syndrome, congenital aniridia, or after refractive surgery, suggesting this molecule as biomarker for dry eye condition. At the intraocular level, some diadenosine polyphosphates are abnormally elevated in glaucoma patients, and this can be related to the stimulation of a P2Y 2 receptor that increases the chloride efflux and water movement in the ciliary epithelium. In the retina, the dinucleotide dCp 4 U, has been proven to be useful to help in the recovery of retinal detachments. Altogether, dinucleoside polyphosphates are a group of compounds which present relevant physiological actions but which also can perform promising therapeutic benefits.

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“…ApaA/Ap3 A seem to be implicated in cell metabolic pathways [3,4]. The ability to catalyze ApnA and Ap3A synthesis was first reported for lysyl-tRNA synthetase from E. coli [5]. Later some other aaRS of different origin and amino acid specificity were shown to synthesize such dinucleoside oligophosphates in vitro (see [3]).…”

Section: Introductionmentioning

confidence: 99%

P¹, P³‐bis(5′‐adenosyl)triphosphate (Ap₃A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase

1994

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Bovine tryptophanyl-tRNA synthetase (TrpRS, E.C. 6.1.1.2) is unable to catalyze in vitro formation of Ap4A in contrast to some other aminoacyltRNA synthetases. However, in the presence of L-tryptophan, ATP-Mg 2÷ and ADP the enzyme catalyzes the Ap3A synthesis via adenylate intermediate. Ap3A (not Ap4A) may serve as a substrate for TrpRS in the reaction of E. (Trp ~ AMP) formation and in the tRNA Tw charging. The Km value for Ap3A was higher than the Km for ATP (approx. 1.00 vs. 0.22 mM) and Vm~x was 3 times lower than for ATP. The Zn2+-deficient enzyme catalyzes Ap3A synthesis in the absence of exogenous ADP due to ATPase activity of Zn2+-deprived TrpRS. The inability of mammalian TrpRS to synthesize Ap4A, might be considered as a molecular tool preventing the removal of Zn 2÷ due to chelation by Ap4A and therefore preserving the enzyme activity.

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Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase

Cited by 266 publications

References 3 publications

Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

The role of dinucleoside polyphosphates on the ocular surface and other eye structures

P¹, P³‐bis(5′‐adenosyl)triphosphate (Ap₃A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase

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Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase

Cited by 266 publications

References 3 publications

Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

The role of dinucleoside polyphosphates on the ocular surface and other eye structures

P1, P3‐bis(5′‐adenosyl)triphosphate (Ap3A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase

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P¹, P³‐bis(5′‐adenosyl)triphosphate (Ap₃A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase