A Novel N-Methyltransferase in Arabidopsis Appears to Feed a Conserved Pathway for Nicotinate Detoxification among Land Plants and Is Associated with Lignin Biosynthesis . Issue 3 (22nd May 2017)
- Record Type:
- Journal Article
- Title:
- A Novel N-Methyltransferase in Arabidopsis Appears to Feed a Conserved Pathway for Nicotinate Detoxification among Land Plants and Is Associated with Lignin Biosynthesis . Issue 3 (22nd May 2017)
- Main Title:
- A Novel N-Methyltransferase in Arabidopsis Appears to Feed a Conserved Pathway for Nicotinate Detoxification among Land Plants and Is Associated with Lignin Biosynthesis
- Authors:
- Li, Wei
Zhang, Fengxia
Wu, Ranran
Jia, Lijia
Li, Guosheng
Guo, Yalong
Liu, Cuimin
Wang, Guodong - Abstract:
- Abstract : N-Methylated nicotinate, produced by NANMT and COMT, is a conserved nicotinate detoxification in land plants. Abstract: The Preiss-Handler pathway, which salvages nicotinate (NA ) for NAD synthesis, is an indispensable biochemical pathway in land plants. Various NA conjugations (mainly methylation and glycosylation) have been detected and have long been proposed for NA detoxification in plants. Previously, we demonstrated that NA O -glucosylation functions as a mobilizable storage form for NAD biosynthesis in the Brassicaceae. However, little is known about the functions of other NA conjugations in plants. In this study, we first found that N -methylnicotinate is a ubiquitous NA conjugation in land plants. Furthermore, we functionally identified a novel methyltransferase (At3g53140; NA N MT), which is mainly responsible for N -methylnicotinate formation, from Arabidopsis ( Arabidopsis thaliana ). We also established that trigonelline is a detoxification form of endogenous NA in plants. Combined phylogenetic analysis and enzymatic assays revealed that NA N -methylation activity was likely derived from the duplication and subfunctionalization of an ancestral caffeic acid O -methyltransferase ( COMT ) gene in the course of land plant evolution. COMT enzymes, which function in S -lignin biosynthesis, also have weak NA N MT activity. Our data suggest that NA detoxification conferred by NA N MT and COMT might have facilitated the retention of the Preiss-HandlerAbstract : N-Methylated nicotinate, produced by NANMT and COMT, is a conserved nicotinate detoxification in land plants. Abstract: The Preiss-Handler pathway, which salvages nicotinate (NA ) for NAD synthesis, is an indispensable biochemical pathway in land plants. Various NA conjugations (mainly methylation and glycosylation) have been detected and have long been proposed for NA detoxification in plants. Previously, we demonstrated that NA O -glucosylation functions as a mobilizable storage form for NAD biosynthesis in the Brassicaceae. However, little is known about the functions of other NA conjugations in plants. In this study, we first found that N -methylnicotinate is a ubiquitous NA conjugation in land plants. Furthermore, we functionally identified a novel methyltransferase (At3g53140; NA N MT), which is mainly responsible for N -methylnicotinate formation, from Arabidopsis ( Arabidopsis thaliana ). We also established that trigonelline is a detoxification form of endogenous NA in plants. Combined phylogenetic analysis and enzymatic assays revealed that NA N -methylation activity was likely derived from the duplication and subfunctionalization of an ancestral caffeic acid O -methyltransferase ( COMT ) gene in the course of land plant evolution. COMT enzymes, which function in S -lignin biosynthesis, also have weak NA N MT activity. Our data suggest that NA detoxification conferred by NA N MT and COMT might have facilitated the retention of the Preiss-Handler pathway in land plants. … (more)
- Is Part Of:
- Plant physiology. Volume 174:Issue 3(2017)
- Journal:
- Plant physiology
- Issue:
- Volume 174:Issue 3(2017)
- Issue Display:
- Volume 174, Issue 3 (2017)
- Year:
- 2017
- Volume:
- 174
- Issue:
- 3
- Issue Sort Value:
- 2017-0174-0003-0000
- Page Start:
- 1492
- Page End:
- 1504
- Publication Date:
- 2017-05-22
- 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.17.00259 ↗
- 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:
- 16617.xml