title: Transcriptional and physiological changes in the S assimilation pathway due to single or combined S and Fe deprivation in durum wheat (Triticum durum L.) seedlings.
abstract: The effect of iron (Fe) and sulphur (S) deprivation on sulphate uptake and assimilation pathways was investigated in durum wheat by analysing the expression of genes coding for major transporters and enzymes involved in sulphate assimilation and reduction: high-affinity sulphate transporters (TdSultr1.1 and TdSultr1.3), ATP sulphurylase (TdATPSul1 and TdATPSul2), APS reductase (TdAPR), sulphite reductase (TdSiR), O-acetylserine(thiol)lyase (TdOASTL1 and TdOASTL2), and serine acetyltransferase (TdSAT1 and TdSAT2). Further experiments were carried out to detect changes in the activities of these enzymes, together with the evaluation of growth parameters (fresh biomass accumulation, leaf green values, and total S, thiol, and Fe concentrations). Fe shortage in wheat plants under adequate S nutrition resulted in an S deficiency-like response. Most of the genes of the S assimilatory pathway induced by S deprivation (TdATPSul1, TdAPR, TdSir, TdSAT1, and TdSAT2) were also significantly up-regulated after the imposition of the Fe limitation under S-sufficient conditions. However, the differential expression of genes encoding the two high-affinity transporters (TdSultr1.1 and TdSultr1.3) indicates that the mechanisms of sulphate uptake regulation under Fe and S deficiency are different in wheat. Moreover, it was observed that the mRNA level of genes encoding ATPS, APR, and OASTL and the corresponding enzyme activities were often uncoupled in response to Fe and S availability, indicating that most probably their regulation involves a complex interplay of transcriptional, translational, and/or post-translational mechanisms induced by S and/or Fe deficiency.
authors: Department of Agriculture, Forests, Nature and Energy (DAFNE), University of Tuscia, 01100 Viterbo, Italy.
authors: Mario
authors: M
authors: Ciaffi
authors: Anna Rita
authors: AR
authors: Paolacci
authors: Silvia
authors: S
authors: Celletti
authors: Giulio
authors: G
authors: Catarcione
authors: Stanislav
authors: S
authors: Kopriva
authors: Stefania
authors: S
authors: Astolfi
mesh_terms: D001692:Biological Transport; D003001:Cloning, Molecular; D004789:Enzyme Activation; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D007501:Iron / Q000378:metabolism*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000235:genetics / Q000378:metabolism; D018515:Plant Leaves / Q000201:enzymology / Q000502:physiology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D018517:Plant Roots / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D018749:RNA, Plant / Q000235:genetics / Q000378:metabolism*; D036226:Seedlings / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D051050:Serine O-Acetyltransferase / Q000235:genetics / Q000378:metabolism; D013312:Stress, Physiological; D013430:Sulfate Adenylyltransferase / Q000235:genetics / Q000378:metabolism; D013431:Sulfates / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism*; D014158:Transcription, Genetic; D014908:Triticum / Q000201:enzymology / Q000235:genetics / Q000502:physiology*
chemical_list: D010940:Plant Proteins; D012333:RNA, Messenger; D018749:RNA, Plant; D013431:Sulfates; D013455:Sulfur; D007501:Iron; D050862:Oxidoreductases Acting on Sulfur Group Donors; C019618:adenylylsulfate reductase; D051050:Serine O-Acetyltransferase; D013430:Sulfate Adenylyltransferase
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