Biochemical Principles and Functional Aspects of Pipecolic Acid Biosynthesis in Plant Immunity. Issue 1 (22nd March 2017)
- Record Type:
- Journal Article
- Title:
- Biochemical Principles and Functional Aspects of Pipecolic Acid Biosynthesis in Plant Immunity. Issue 1 (22nd March 2017)
- Main Title:
- Biochemical Principles and Functional Aspects of Pipecolic Acid Biosynthesis in Plant Immunity
- Authors:
- Hartmann, Michael
Kim, Denis
Bernsdorff, Friederike
Ajami-Rashidi, Ziba
Scholten, Nicola
Schreiber, Stefan
Zeier, Tatyana
Schuck, Stefan
Reichel-Deland, Vanessa
Zeier, Jürgen - Abstract:
- Abstract : The immune regulator pipecolic acid is synthesized by ALD1-mediated conversion of l -Lys to 2, 3-dehydropipecolic acid and consecutive reduction, to which Arabidopsis SARD4/ORNCD1 largely contributes. Abstract: The nonprotein amino acid pipecolic acid (Pip ) regulates plant systemic acquired resistance and basal immunity to bacterial pathogen infection. In Arabidopsis ( Arabidopsis thaliana ), the lysine (Lys) aminotransferase AGD2-LIKE DEFENSE RESPONSE PROTEIN1 (ALD1) mediates the pathogen-induced accumulation of Pip in inoculated and distal leaf tissue. Here, we show that ALD1 transfers the α-amino group of l -Lys to acceptor oxoacids. Combined mass spectrometric and infrared spectroscopic analyses of in vitro assays and plant extracts indicate that the final product of the ALD1-catalyzed reaction is enaminic 2, 3-dehydropipecolic acid (DP ), whose formation involves consecutive transamination, cyclization, and isomerization steps. Besides l -Lys, recombinant ALD1 transaminates l -methionine, l -leucine, diaminopimelate, and several other amino acids to generate oxoacids or derived products in vitro. However, detailed in planta analyses suggest that the biosynthesis of 2, 3-DP from l -Lys is the major in vivo function of ALD1. Since ald1 mutant plants are able to convert exogenous 2, 3-DP into Pip, their Pip deficiency relies on the inability to form the 2, 3-DP intermediate. The Arabidopsis reductase ornithine cyclodeaminase/μ-crystallin, alias SYSTEMICAbstract : The immune regulator pipecolic acid is synthesized by ALD1-mediated conversion of l -Lys to 2, 3-dehydropipecolic acid and consecutive reduction, to which Arabidopsis SARD4/ORNCD1 largely contributes. Abstract: The nonprotein amino acid pipecolic acid (Pip ) regulates plant systemic acquired resistance and basal immunity to bacterial pathogen infection. In Arabidopsis ( Arabidopsis thaliana ), the lysine (Lys) aminotransferase AGD2-LIKE DEFENSE RESPONSE PROTEIN1 (ALD1) mediates the pathogen-induced accumulation of Pip in inoculated and distal leaf tissue. Here, we show that ALD1 transfers the α-amino group of l -Lys to acceptor oxoacids. Combined mass spectrometric and infrared spectroscopic analyses of in vitro assays and plant extracts indicate that the final product of the ALD1-catalyzed reaction is enaminic 2, 3-dehydropipecolic acid (DP ), whose formation involves consecutive transamination, cyclization, and isomerization steps. Besides l -Lys, recombinant ALD1 transaminates l -methionine, l -leucine, diaminopimelate, and several other amino acids to generate oxoacids or derived products in vitro. However, detailed in planta analyses suggest that the biosynthesis of 2, 3-DP from l -Lys is the major in vivo function of ALD1. Since ald1 mutant plants are able to convert exogenous 2, 3-DP into Pip, their Pip deficiency relies on the inability to form the 2, 3-DP intermediate. The Arabidopsis reductase ornithine cyclodeaminase/μ-crystallin, alias SYSTEMIC ACQUIRED RESISTANCE-DEFICIENT4 (SARD4), converts ALD1-generated 2, 3-DP into Pip in vitro. SARD4 significantly contributes to the production of Pip in pathogen-inoculated leaves but is not the exclusive reducing enzyme involved in Pip biosynthesis. Functional SARD4 is required for proper basal immunity to the bacterial pathogen Pseudomonas syringae . Although SARD4 knockout plants show greatly reduced accumulation of Pip in leaves distal to P. syringae inoculation, they display a considerable systemic acquired resistance response. This suggests a triggering function of locally accumulating Pip for systemic resistance induction. … (more)
- Is Part Of:
- Plant physiology. Volume 174:Issue 1(2017)
- Journal:
- Plant physiology
- Issue:
- Volume 174:Issue 1(2017)
- Issue Display:
- Volume 174, Issue 1 (2017)
- Year:
- 2017
- Volume:
- 174
- Issue:
- 1
- Issue Sort Value:
- 2017-0174-0001-0000
- Page Start:
- 124
- Page End:
- 153
- Publication Date:
- 2017-03-22
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.17.00222 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16197.xml