Arabidopsis ADC1 functions as an Nδ‐acetylornithine decarboxylase. Issue 5 (17th October 2019)
- Record Type:
- Journal Article
- Title:
- Arabidopsis ADC1 functions as an Nδ‐acetylornithine decarboxylase. Issue 5 (17th October 2019)
- Main Title:
- Arabidopsis ADC1 functions as an Nδ‐acetylornithine decarboxylase
- Authors:
- Lou, Yann‐Ru
Ahmed, Sheaza
Yan, Jian
Adio, Adewale M.
Powell, Hannah M.
Morris, Paul F.
Jander, Georg - Abstract:
- Abstract: Polyamines are small aliphatic amines found in almost all organisms, ranging from bacteria to plants and animals. In most plants, putrescine, the metabolic precursor for longer polyamines, such as spermidine and spermine, is produced from arginine, with either agmatine or ornithine as intermediates. Here we show that Arabidopsis thaliana ( Arabidopsis ) arginine decarboxylase 1 (ADC1), one of the two known arginine decarboxylases in Arabidopsis, not only synthesizes agmatine from arginine, but also converts N δ ‐ acetylornithine to N ‐acetylputrescine. Phylogenetic analyses indicate that duplication and neofunctionalization of ADC1 and NATA1, the enzymes that synthesize N δ ‐ acetylornithine in Arabidopsis, co‐occur in a small number of related species in the Brassicaceae. Unlike ADC2, which is localized in the chloroplasts, ADC1 is in the endoplasmic reticulum together with NATA1, an indication that these two enzymes have access to the same substrate pool. Together, these results are consistent with a model whereby NATA1 and ADC1 together provide a pathway for the synthesis of N‐ acetylputrescine in Arabidopsis . Abstract : An arginine decarboxylase in Arabidopsis was shown to function as an N‐delta‐acetylornithine decarboxylase as well, leading to the formation of N‐acetylputrescine. This enzymatic activity provides a route for the formation of acetylated polyamines. Polyamine acetylation may facilitate transport across membranes and function in plant stressAbstract: Polyamines are small aliphatic amines found in almost all organisms, ranging from bacteria to plants and animals. In most plants, putrescine, the metabolic precursor for longer polyamines, such as spermidine and spermine, is produced from arginine, with either agmatine or ornithine as intermediates. Here we show that Arabidopsis thaliana ( Arabidopsis ) arginine decarboxylase 1 (ADC1), one of the two known arginine decarboxylases in Arabidopsis, not only synthesizes agmatine from arginine, but also converts N δ ‐ acetylornithine to N ‐acetylputrescine. Phylogenetic analyses indicate that duplication and neofunctionalization of ADC1 and NATA1, the enzymes that synthesize N δ ‐ acetylornithine in Arabidopsis, co‐occur in a small number of related species in the Brassicaceae. Unlike ADC2, which is localized in the chloroplasts, ADC1 is in the endoplasmic reticulum together with NATA1, an indication that these two enzymes have access to the same substrate pool. Together, these results are consistent with a model whereby NATA1 and ADC1 together provide a pathway for the synthesis of N‐ acetylputrescine in Arabidopsis . Abstract : An arginine decarboxylase in Arabidopsis was shown to function as an N‐delta‐acetylornithine decarboxylase as well, leading to the formation of N‐acetylputrescine. This enzymatic activity provides a route for the formation of acetylated polyamines. Polyamine acetylation may facilitate transport across membranes and function in plant stress responses. … (more)
- Is Part Of:
- Journal of integrative plant biology. Volume 62:Issue 5(2020)
- Journal:
- Journal of integrative plant biology
- Issue:
- Volume 62:Issue 5(2020)
- Issue Display:
- Volume 62, Issue 5 (2020)
- Year:
- 2020
- Volume:
- 62
- Issue:
- 5
- Issue Sort Value:
- 2020-0062-0005-0000
- Page Start:
- 601
- Page End:
- 613
- Publication Date:
- 2019-10-17
- Subjects:
- Plants -- Periodicals
Plants -- China -- Periodicals
Electronic journals
580.5 - Journal URLs:
- http://bibpurl.oclc.org/web/10380 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1744-7909 ↗
http://www.blackwell-synergy.com/loi/jipb ↗
http://www.blackwell-synergy.com/openurl?genre=journal&eissn=1744-7909 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/jipb.12821 ↗
- Languages:
- English
- ISSNs:
- 1672-9072
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5007.538427
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13285.xml