It is known that cells under stress accumulate various dinucleoside polyphosphates, compounds suggested to function as alarmones. In plants, the phenylpropanoid pathways yield metabolites protecting these organisms against various types of stress. Observations reported in this communication link these two phenomena and provide an example of a metabolic "addressee" for an "alarm" signaled by diadenosine triphosphate (Ap3A) or diadenosine tetraphosphate (Ap4A). In response to added Ap3A or Ap4A, seedlings of Arabidopsis thaliana incubated in full nutrition medium increased both the expression of the genes for and the specific activity of phenylalanine ammonia-lyase and 4-coumarate:coenzyme A ligase, enzymes that control the beginning of the phenylpropanoid pathway. Neither adenine mononucleotides (AMP, ADP or ATP) nor adenosine evoked such effects. Reactions catalyzed in vitro by these enzymes were not affected by Ap3A or Ap4A.
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http://dx.doi.org/10.1016/j.fob.2011.10.002 | DOI Listing |
Nat Commun
October 2021
Department of Chemistry, University of Konstanz, Konstanz, Germany.
The nucleotides diadenosine triphosphate (ApA) and diadenosine tetraphosphate (ApA) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress, they are considered to be alarmones triggering stress adaptive processes. However, their cellular roles remain elusive.
View Article and Find Full Text PDFAnal Biochem
August 2020
Pharmaceutical Institute, Pharmaceutical & Medicinal Chemistry, University of Bonn, An der Immenburg 4, 53121, Bonn, Germany; PharmaCenter Bonn, University of Bonn, An der Immenburg 4, 53121, Bonn, Germany. Electronic address:
Nucleotide pyrophosphatase/phosphodiesterase 4 (NPP4) is a membrane-bound enzyme that hydrolyzes extracellular diadenosine polyphosphates such as diadenosine triphosphate (ApA) and diadenosine tetraphosphate (ApA) yielding mononucleotides. NPP4 on the surface of endothelial cells was reported to promote platelet aggregation by hydrolyzing ApA to ADP, which activates pro-thrombotic G protein-coupled P2Y and P2Y receptors. Thus, NPP4 inhibitors have potential as novel antithrombotic drugs.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
February 2020
Kimmel Center for Biology and Medicine at the Skirball Institute, New York University School of Medicine, New York, NY 10016;
Stresses that increase the cellular concentration of dinucleoside tetraphosphates (NpNs) have recently been shown to impact RNA degradation by inducing nucleoside tetraphosphate (Np) capping of bacterial transcripts. However, neither the mechanism by which such caps are acquired nor the function of NpNs in bacteria is known. Here we report that promoter sequence changes upstream of the site of transcription initiation similarly affect both the efficiency with which RNA polymerase incorporates dinucleoside polyphosphates at the 5' end of nascent transcripts in vitro and the percentage of transcripts that are Np-capped in , clear evidence for Np cap acquisition by NpN incorporation during transcription initiation in bacterial cells.
View Article and Find Full Text PDFPlant Physiol Biochem
February 2020
Department of Biochemistry and Biotechnology, Poznań University of Life Sciences, Dojazd 11, 60-632, Poznań, Poland.
It is known that the concentration of dinucleoside polyphosphates (NpN's) in cells increases under stress and that adverse environmental factors induce biosynthesis of phenylpropanoids, which protect the plant against stress. Previously, we showed that purine NpN's such as ApA and ApA induce both the activity of enzymes of the phenylpropanoid pathway and the expression of relevant genes in Arabidopsis seedlings. Moreover, we showed that ApA induced stilbene biosynthesis in Vitis vinifera cv.
View Article and Find Full Text PDFCell Chem Biol
November 2019
Department of Chemistry, Konstanz Research School Chemical Biology, University of Konstanz, Universitätsstrasse 10, 78464 Konstanz, Germany. Electronic address:
Diadenosine polyphosphates (ApAs) such as diadenosine tri- and tetraphosphates are formed in prokaryotic as well as eukaryotic cells. Since upon stress intracellular ApA concentrations increase, it was postulated that ApAs are alarmones triggering stress-adaptive processes. The major synthesis pathway of ApAs is assumed to be a side reaction of amino acid activation.
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