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The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation

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Standard

The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation. / Deuschle, Karen; Funck, Dietmar; Forlani, Giuseppe; Stransky, Harald; Biehl, Alexander; Leister, Dario; van der Graaff, Eric; Kunze, Reinhard; Frommer, Wolf B.

I: Plant Cell, Bind 16, Nr. 12, 12.2004, s. 3413-25.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Deuschle, K, Funck, D, Forlani, G, Stransky, H, Biehl, A, Leister, D, van der Graaff, E, Kunze, R & Frommer, WB 2004, 'The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation', Plant Cell, bind 16, nr. 12, s. 3413-25. https://doi.org/10.1105/tpc.104.023622

APA

Deuschle, K., Funck, D., Forlani, G., Stransky, H., Biehl, A., Leister, D., ... Frommer, W. B. (2004). The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation. Plant Cell, 16(12), 3413-25. https://doi.org/10.1105/tpc.104.023622

Vancouver

Deuschle K, Funck D, Forlani G, Stransky H, Biehl A, Leister D o.a. The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation. Plant Cell. 2004 dec;16(12):3413-25. https://doi.org/10.1105/tpc.104.023622

Author

Deuschle, Karen ; Funck, Dietmar ; Forlani, Giuseppe ; Stransky, Harald ; Biehl, Alexander ; Leister, Dario ; van der Graaff, Eric ; Kunze, Reinhard ; Frommer, Wolf B. / The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation. I: Plant Cell. 2004 ; Bind 16, Nr. 12. s. 3413-25.

Bibtex

@article{28f4fe0b6c9a4d5a96c65fe9408ff61d,
title = "The role of Δ1-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.",
keywords = "1-Pyrroline-5-Carboxylate Dehydrogenase, Aldehyde Oxidoreductases, Apoptosis, Arabidopsis, Arabidopsis Proteins, Arginine, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Glutamate-5-Semialdehyde Dehydrogenase, Glutamic Acid, Mutation, Ornithine, Oxidoreductases Acting on CH-NH Group Donors, Proline, Reactive Oxygen Species, Salicylic Acid, Signal Transduction",
author = "Karen Deuschle and Dietmar Funck and Giuseppe Forlani and Harald Stransky and Alexander Biehl and Dario Leister and {van der Graaff}, Eric and Reinhard Kunze and Frommer, {Wolf B}",
year = "2004",
month = "12",
doi = "10.1105/tpc.104.023622",
language = "English",
volume = "16",
pages = "3413--25",
journal = "The Plant Cell",
issn = "1040-4651",
publisher = "American Society of Plant Biologists",
number = "12",

}

RIS

TY - JOUR

T1 - The role of Δ1-pyrroline-5-carboxylate dehydrogenase in proline degradation

AU - Deuschle, Karen

AU - Funck, Dietmar

AU - Forlani, Giuseppe

AU - Stransky, Harald

AU - Biehl, Alexander

AU - Leister, Dario

AU - van der Graaff, Eric

AU - Kunze, Reinhard

AU - Frommer, Wolf B

PY - 2004/12

Y1 - 2004/12

N2 - 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.

AB - 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.

KW - 1-Pyrroline-5-Carboxylate Dehydrogenase

KW - Aldehyde Oxidoreductases

KW - Apoptosis

KW - Arabidopsis

KW - Arabidopsis Proteins

KW - Arginine

KW - Gene Expression Regulation, Enzymologic

KW - Gene Expression Regulation, Plant

KW - Glutamate-5-Semialdehyde Dehydrogenase

KW - Glutamic Acid

KW - Mutation

KW - Ornithine

KW - Oxidoreductases Acting on CH-NH Group Donors

KW - Proline

KW - Reactive Oxygen Species

KW - Salicylic Acid

KW - Signal Transduction

U2 - 10.1105/tpc.104.023622

DO - 10.1105/tpc.104.023622

M3 - Journal article

C2 - 15548746

VL - 16

SP - 3413

EP - 3425

JO - The Plant Cell

JF - The Plant Cell

SN - 1040-4651

IS - 12

ER -

ID: 106391401