title: Cytosolic protons as secondary messengers in elicitor-induced defence responses.
abstract: A variety of early elicitor-induced membrane responses have been described, and their possible role in the generation of second messengers involved in the cascades of events leading to the activation of defence genes is actively investigated. Treatment of tobacco cells with a crude elicitor preparation from Phytophthora megasperma, purified oligouronides and a commercial pectate lyase, induce a common set of membrane reactions similar to those described in a variety of plant material, i.e. efflux of K+, extracellular alkalinization, net Ca2+ uptake and membrane depolarization. In the same conditions the three elicitors stimulate the activity of phenylalanine ammonia-lyase (PAL) and O-diphenol methyltransferase (OMT), two enzymes of the phenylpropanoid pathway. A good correlation between the intensity of the membrane response and the extent of enzyme stimulation has been observed. Cytosolic acidifications have also been measured as a rapid response to the different elicitor preparations used. These results show that plant cells (which usually succeed in counteracting pH-perturbing processes associated with their metabolism, with the transport of solutes or with the effect of various factors from the environment) display significant variation in the concentration of cytosolic protons in specific physiological circumstances, such as the perception of signals inducing defence reactions. Direct evidence that these cytosolic pH changes could be interpreted by plant cells as messages involved in triggering defence responses is provided by experiments showing that artificial acidifications of the cytoplasm lead to a co-ordinated stimulation of PAL and OMT. These results stress the need to explore in more detail the role played by cytoplasmic mechanisms underlying those pH changes.
authors.affiliation: C.N.R.S. Institut des Sciences Végétales, Gif-sur-Yvette, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Mathieu
authors.forename: J P
authors.initials: JP
authors.lastname: Jouanneau
authors.forename: S
authors.initials: S
authors.lastname: Thomine
authors.forename: D
authors.initials: D
authors.lastname: Lapous
authors.forename: J
authors.initials: J
authors.lastname: Guern
mesh_terms: D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D002478:Cells, Cultured; D003600:Cytosol / Q000201:enzymology / Q000378:metabolism*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D017136:Ion Transport; D008780:Methyltransferases / Q000378:metabolism; D010650:Phenylalanine Ammonia-Lyase / Q000378:metabolism; D010666:Phenylpropionates / Q000378:metabolism; D010838:Phytophthora / Q000502:physiology; D010947:Plants, Toxic; D011133:Polysaccharide-Lyases / Q000494:pharmacology; D011188:Potassium / Q000378:metabolism; D011522:Protons; D015290:Second Messenger Systems; D014026:Nicotiana / Q000187:drug effects / Q000201:enzymology / Q000276:immunology / Q000378:metabolism*; D014574:Uronic Acids / Q000494:pharmacology
chemical_list: D010666:Phenylpropionates; D011522:Protons; D014574:Uronic Acids; D008780:Methyltransferases; C019608:caffeate O-methyltransferase; D011133:Polysaccharide-Lyases; C023911:pectate lyase; D010650:Phenylalanine Ammonia-Lyase; D011188:Potassium