title: NO-Mediated [Ca2+]cyt Increases Depend on ADP-Ribosyl Cyclase Activity in Arabidopsis.
abstract: Cyclic ADP ribose (cADPR) is a Ca(2+)-mobilizing intracellular second messenger synthesized from NAD by ADP-ribosyl cyclases (ADPR cyclases). In animals, cADPR targets the ryanodine receptor present in the sarcoplasmic/endoplasmic reticulum to promote Ca(2+) release from intracellular stores to increase the concentration of cytosolic free Ca(2+) in Arabidopsis (Arabidopsis thaliana), and cADPR has been proposed to play a central role in signal transduction pathways evoked by the drought and stress hormone, abscisic acid, and the circadian clock. Despite evidence for the action of cADPR in Arabidopsis, no predicted proteins with significant similarity to the known ADPR cyclases have been reported in any plant genome database, suggesting either that there is a unique route for cADPR synthesis or that a homolog of ADPR cyclase with low similarity might exist in plants. We sought to determine whether the low levels of ADPR cyclase activity reported in Arabidopsis are indicative of a bona fide activity that can be associated with the regulation of Ca(2+) signaling. We adapted two different fluorescence-based assays to measure ADPR cyclase activity in Arabidopsis and found that this activity has the characteristics of a nucleotide cyclase that is activated by nitric oxide to increase cADPR and mobilize Ca(2.)
authors.affiliation: Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom (S.M.A.-A., C.T.H., M.P.D., A.G.S., A.A.R.W.);Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh (S.M.A.-A.);Department of Biochemistry, University of Sao Paulo, Sao Paulo, CEP 05508/000, Brazil (C.T.H.); andSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom (A.N.D.).
authors.forename: S M
authors.identifier: 0000-0002-8807-624X
authors.initials: SM
authors.lastname: Abdul-Awal
authors.affiliation: Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom (S.M.A.-A., C.T.H., M.P.D., A.G.S., A.A.R.W.);Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh (S.M.A.-A.);Department of Biochemistry, University of Sao Paulo, Sao Paulo, CEP 05508/000, Brazil (C.T.H.); andSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom (A.N.D.).
authors.forename: Carlos T
authors.initials: CT
authors.lastname: Hotta
authors.affiliation: Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom (S.M.A.-A., C.T.H., M.P.D., A.G.S., A.A.R.W.);Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh (S.M.A.-A.);Department of Biochemistry, University of Sao Paulo, Sao Paulo, CEP 05508/000, Brazil (C.T.H.); andSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom (A.N.D.).
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Davey
authors.affiliation: Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom (S.M.A.-A., C.T.H., M.P.D., A.G.S., A.A.R.W.);Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh (S.M.A.-A.);Department of Biochemistry, University of Sao Paulo, Sao Paulo, CEP 05508/000, Brazil (C.T.H.); andSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom (A.N.D.).
authors.forename: Antony N
authors.initials: AN
authors.lastname: Dodd
authors.affiliation: Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom (S.M.A.-A., C.T.H., M.P.D., A.G.S., A.A.R.W.);Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh (S.M.A.-A.);Department of Biochemistry, University of Sao Paulo, Sao Paulo, CEP 05508/000, Brazil (C.T.H.); andSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom (A.N.D.).
authors.forename: Alison G
authors.identifier: 0000-0001-6511-5704
authors.initials: AG
authors.lastname: Smith
authors.affiliation: Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom (S.M.A.-A., C.T.H., M.P.D., A.G.S., A.A.R.W.);Biotechnology and Genetic Engineering Discipline, Khulna University, Khulna 9208, Bangladesh (S.M.A.-A.);Department of Biochemistry, University of Sao Paulo, Sao Paulo, CEP 05508/000, Brazil (C.T.H.); andSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom (A.N.D.) aarw2@cam.ac.uk.
authors.forename: Alex A R
authors.identifier: 0000-0003-0261-4375
authors.initials: AA
authors.lastname: Webb
mesh_terms: D036541:ADP-ribosyl Cyclase / Q000378:metabolism*; D017360:Arabidopsis / Q000187:drug effects / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism; D002118:Calcium / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D006150:Guanine Nucleotides / Q000378:metabolism; D009243:NAD / Q000031:analogs & derivatives / Q000378:metabolism; D009536:Niacinamide / Q000494:pharmacology; D009569:Nitric Oxide / Q000378:metabolism*; D015398:Signal Transduction / Q000187:drug effects
chemical_list: D029681:Arabidopsis Proteins; D006150:Guanine Nucleotides; D009243:NAD; C032140:nicotinamide-hypoxanthine dinucleotide; D009536:Niacinamide; D009569:Nitric Oxide; C102728:nicotinamide guanine dinucleotide; D036541:ADP-ribosyl Cyclase; D002118:Calcium