title: The role of [Delta]1-pyrroline-5-carboxylate dehydrogenase in proline degradation.
abstract: In response to stress, plants accumulate Pro, requiring degradation after release from adverse conditions. Delta1-Pyrroline-5-carboxylate dehydrogenase (P5CDH), the second enzyme for Pro degradation, is encoded by a single gene expressed ubiquitously. To study the physiological function of P5CDH, T-DNA insertion mutants in AtP5CDH were isolated and characterized. Although Pro degradation was undetectable in p5cdh mutants, neither increased Pro levels nor an altered growth phenotype were observed under normal conditions. Thus AtP5CDH is essential for Pro degradation but not required for vegetative plant growth. External Pro application caused programmed cell death, with callose deposition, reactive oxygen species production, and DNA laddering, involving a salicylic acid signal transduction pathway. p5cdh mutants were hypersensitive toward Pro and other molecules producing P5C, such as Arg and Orn. Pro levels were the same in the wild type and mutants, but P5C was detectable only in p5cdh mutants, indicating that P5C accumulation may be the cause for Pro hypersensitivity. Accordingly, overexpression of AtP5CDH resulted in decreased sensitivity to externally supplied Pro. Thus, Pro and P5C/Glu semialdehyde may serve as a link between stress responses and cell death.
authors.affiliation: Plant Physiology, Zentrum für Molekularbiologie der Pflanzen, Pflanzenphysiologie, Universität Tübingen, D-72076 Tübingen, Germany.
authors.forename: Karen
authors.initials: K
authors.lastname: Deuschle
authors.forename: Dietmar
authors.initials: D
authors.lastname: Funck
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Forlani
authors.forename: Harald
authors.initials: H
authors.lastname: Stransky
authors.forename: Alexander
authors.initials: A
authors.lastname: Biehl
authors.forename: Dario
authors.initials: D
authors.lastname: Leister
authors.forename: Eric
authors.initials: E
authors.lastname: van der Graaff
authors.forename: Reinhard
authors.initials: R
authors.lastname: Kunze
authors.forename: Wolf B
authors.initials: WB
authors.lastname: Frommer
mesh_terms: D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D017360:Arabidopsis / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001120:Arginine / Q000378:metabolism / Q000494:pharmacology; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects / Q000235:genetics; D018506:Gene Expression Regulation, Plant / Q000187:drug effects / Q000235:genetics; D050698:Glutamate-5-Semialdehyde Dehydrogenase; D018698:Glutamic Acid / Q000378:metabolism; D009154:Mutation / Q000235:genetics; D009952:Ornithine / Q000378:metabolism / Q000494:pharmacology; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000235:genetics / Q000378:metabolism*; D011392:Proline / Q000378:metabolism* / Q000494:pharmacology; D017382:Reactive Oxygen Species / Q000378:metabolism; D020156:Salicylic Acid / Q000378:metabolism; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology
chemical_list: D029681:Arabidopsis Proteins; D017382:Reactive Oxygen Species; D018698:Glutamic Acid; D001120:Arginine; D011392:Proline; D009952:Ornithine; D000445:Aldehyde Oxidoreductases; D050698:Glutamate-5-Semialdehyde Dehydrogenase; D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D020156:Salicylic Acid