6533b859fe1ef96bd12b6fb0
RESEARCH PRODUCT
The plasma membrane oxidase NtrbohD is responsible for AOS production in elicited tobacco cells
Jean-pierre BleinFrançoise Simon-plasTaline Elmayansubject
0106 biological sciencesTime FactorsNicotiana tabacumMolecular Sequence DataPlant ScienceBiologyGenes Plant01 natural sciencesFungal Proteins[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciences[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsComplementary DNATobaccoGene expressionGeneticsExtracellularAOSAmino Acid SequenceRNA MessengerCells CulturedComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesOxidase testNADPH oxidaseGene Expression ProfilingAlgal ProteinsCell MembraneHydrogen PeroxideCell BiologyHydrogen-Ion ConcentrationPlants Genetically Modifiedbiology.organism_classification3. Good healthElicitorCell biologyPlant LeavesProtein TransportBiochemistryCell culturebiology.proteinOxidoreductasesReactive Oxygen Species010606 plant biology & botanydescription
Summary A cDNA encoding a protein, NtrbohD, located on the plasma membrane and homologue to the flavocytochrome of the neutrophil NADPH oxidase, was cloned in tobacco. The corresponding mRNA was accumulated when tobacco leaves and cells were treated with the fungal elicitor cryptogein. After elicitation with cryptogein, tobacco cells transformed with antisense constructs of NtrbohD showed the same extracellular alkalinization as the control, but no longer produced active oxygen species (AOS). This work represents the first demonstration of the function of a homologue of gp91–phox in AOS production in elicited tobacco cells.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-01-01 |