[Nucleoside polyphosphates: occurrence, metabolism and function].

K Riedel

doi:10.1002/jobm.3630230206

Home/Archive/PubMed

PubMed · 6346704

[Nucleoside polyphosphates: occurrence, metabolism and function].

K Riedel

View original source ↗Export metadata ↓

Abstract

Procaryotes have regulatory systems allowing to vary the metabolism in response to nutritional variations, to reduce the growth, and to start development. Nucleoside polyphosphates are mediators of coordinated alterations of metabolism. In this review, after a brief recall of the characteristics of the stringent response, the occurrence, determinations, and the metabolism of the nucleoside polyphosphates are presented. The representation of the pleiotropic effects includes the regulation of the protein synthesis and of the protein synthesis apparatus, of the protein turnover, of the N- and carbohydrate metabolism, of the formation of cell membranes and cell walls as well as the possible function of the development.

Explore related subjects

Adenine Nucleotides Amino Acids Bacteria Bacterial Proteins Carbohydrate Metabolism Cell Membrane Cell Wall Chemical Phenomena Chemistry Fungal Proteins Fungi Guanine Nucleotides Guanosine Tetraphosphate Nitrogen Fixation Nucleotides Ribosomes English Abstract Journal Article Review

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

K Riedel. 1983. [Nucleoside polyphosphates: occurrence, metabolism and function].. https://doi.org/10.1002/jobm.3630230206

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1995

Peptide probe of ryanodine receptor function. Imperatoxin A, a peptide from the venom of the scorpion Pandinus imperator, selectively activates skeletal-type ryanodine receptor isoforms.

We have used [3H]ryanodine binding experiments and single channel recordings to provide convergent descriptions of the effect of imperatoxin A (IpTxa), a approximately 5-kDa peptide from the venom of the scorpion Pandinus imperator (Valdivia, H. H., Kirby, M. S., Lederer, W. J., and Coronado, R. (1992) Proc. Ntl. Acad. Sc. U.S.A. 89, 12185-12189) on Ca2+ release channels/ryanodine receptors (RyR) of sarcoplasmic reticulum (SR). At nanomolar concentrations, IpTxa increased the binding of [3H]ryanodine to skeletal SR and, to a lesser extent, to cerebellum microsomes. The activating effect of IpTxa on skeletal SR was Ca(2+)-dependent, synergized by caffeine, and independent of other modulators of RyRs. However, IpTxa had negligible effects on tissues where the expression of skeletal-type RyR isoforms (RyR1) is small or altogether absent, i.e. cardiac, cerebrum, and liver microsomes. Thus, IpTxa may be used as a ligand capable of discriminating between RyR isoforms with nanomolar affinity. IpTxa increased the open probability (Po) of rabbit skeletal muscle RyRs by increasing the frequency of open events and decreasing the duration of the closed lifetimes. This activating effect was dose-dependent (ED50 = 10 nM), had a fast onset, and was fully reversible. Purified RyR from solubilized skeletal SR displayed high affinity for [3H]ryanodine with a KD of 6.1 nM and Bmax of approximately 30 pmol/mg of protein. IpTxa increased [3H]ryanodine binding noncompetitively by increasing Bmax to approximately 60 pmol/mg of protein. These results suggested the presence of an IpTxa-binding site on the RyR or a closely associated regulatory protein. This site appears to be distinct from the caffeine- and adenine nucleotide-regulatory sites. IpTxa may prove a useful tool to identify regulatory domains critical for channel gating and to dissect the contribution of skeletal-type RyRs to intracellular Ca2+ waveforms generated by stimulation of different RyR isoforms.

Adenine Nucleotides↗

PubMed1995

Developmental changes of the adenine nucleotide translocation in rat brain.

The perinatal development of the adenine nucleotide translocation in isolated rat brain mitochondria was studied. For that purpose the content of the adenine nucleotide translocase (ANT), the activity of adenine nucleotide translocation and the control of the ANT protein over State 3 respiration were estimated. From the newborn to the adult state there was a 4-fold increase in State 3 respiration which was paralleled by a 3-fold increase in the respiratory control ratio. The capacity of uncoupled respiration exceeded that of State 3 respiration in all developmental stages indicating that the activity of oxidative phosphorylation is influenced by that of ANT and/or ATP synthase. The content of the ANT protein, measured as bound pmoles of [3H]atractyloside per mg mitochondrial protein, increased more than 2-fold from birth to adultness in the first three postnatal weeks. The size of the exchangeable matrix (ATP + ADP)-pool was only slightly expanded during the same period. The translocation activity increased 2-fold from the newborn to the adult state and was a linear function of the ANT protein. Control of the ANT protein over State 3 respiration (quantified as flux control coefficient, CJoANT), was remarkable in brain mitochondria from newborn rats (CJoANT = 0.45 +/- 0.15), but declined during further development (CJoANT = 0.11 +/- 0.03, at the 20th day). The obtained results suggest that the postnatal enrichment of the ANT protein in rat brain mitochondria is an essential factor for the development of oxidative phosphorylation capacity in the early postnatal period.

Adenine Nucleotides↗

PubMed1995

Does the sulfhydryl or the adenine moiety of CoA enhance firefly luciferase activity?

Light production by firefly luciferase is limited by product release resulting in flash kinetics. Several compounds (CoA, PPi, and nucleotides) transform the flash-form of light production into continuous light production. The sulfhydryl group of CoA is required; however, since nucleotides are also active, at least two mechanisms (sites) must exist.

Adenine Nucleotides↗