The Role of Δ1-Pyrroline-5-Carboxylate Dehydrogenase in Proline Degradation[W]
Author:
Deuschle Karen12, Funck Dietmar1, Forlani Giuseppe3, Stransky Harald1, Biehl Alexander4, Leister Dario4, van der Graaff Eric5, Kunze Reinhard5, Frommer Wolf B.12
Affiliation:
1. Plant Physiology, Zentrum für Molekularbiologie der Pflanzen, Pflanzenphysiologie, Universität Tübingen, D-72076 Tübingen, Germany 2. Carnegie Institution, Stanford, California 94305 3. Department of Biology, Università di Ferrara, 44100 Ferrara, Italy 4. Max-Planck-Institut für Züchtungsforschung, 50829 Köln, Germany 5. Institut für Botanik, Universität zu Köln, 50931 Köln, Germany
Abstract
AbstractIn response to stress, plants accumulate Pro, requiring degradation after release from adverse conditions. Δ1-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.
Publisher
Oxford University Press (OUP)
Subject
Cell Biology,Plant Science
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