Biochemical characterization in Norway spruce (Picea abies) of SABATH methyltransferases that methylate phytohormones. (May 2018)
- Record Type:
- Journal Article
- Title:
- Biochemical characterization in Norway spruce (Picea abies) of SABATH methyltransferases that methylate phytohormones. (May 2018)
- Main Title:
- Biochemical characterization in Norway spruce (Picea abies) of SABATH methyltransferases that methylate phytohormones
- Authors:
- Chaiprasongsuk, Minta
Zhang, Chi
Qian, Ping
Chen, Xinlu
Li, Guanglin
Trigiano, Robert N.
Guo, Hong
Chen, Feng - Abstract:
- Abstract: Indole-3-acetic acid (IAA), gibberellins (GAs), salicylic acid (SA) and jasmonic acid (JA) exist in methyl ester forms in plants in addition to their free acid forms. The enzymes that catalyze methylation of these carboxylic acid phytohormones belong to a same protein family, the SABATH methyltransferases. While the genes encoding these enzymes have been isolated from a small number of flowering plants, little is known about their occurrence and evolution in non-flowering plants. Here, we report the systematic characterization of the SABATH family from Norway spruce ( Picea abies ), a gymnosperm. The Norway spruce genome contains ten SABATH genes ( PaSABATH1-10 ). Full-length cDNA for each of the ten PaSABATH genes was cloned and expressed in Escherichia coli . Recombinant PaSABATHs were tested for activity with IAA, GA, SA, and JA. Among the ten PaSABATHs, five had activity with one or more of the four substrates. PaSABATH1 and PaSABATH2 had the highest activities with IAA and SA, respectively. PaSABATH4, PaSABATH5 and PaSABATH10 all had JA as a preferred substrate but with notable differences in biochemical properties. The structural basis of PaSABATHs in discriminating various phytohormone substrates was inferred based on structural models of the enzyme-substrate complexes. The phylogeny of PaSABATHs with selected SABATHs from other plants implies that the enzymes methylating IAA are conserved in seed plants whereas the enzymes methylating JA and SA haveAbstract: Indole-3-acetic acid (IAA), gibberellins (GAs), salicylic acid (SA) and jasmonic acid (JA) exist in methyl ester forms in plants in addition to their free acid forms. The enzymes that catalyze methylation of these carboxylic acid phytohormones belong to a same protein family, the SABATH methyltransferases. While the genes encoding these enzymes have been isolated from a small number of flowering plants, little is known about their occurrence and evolution in non-flowering plants. Here, we report the systematic characterization of the SABATH family from Norway spruce ( Picea abies ), a gymnosperm. The Norway spruce genome contains ten SABATH genes ( PaSABATH1-10 ). Full-length cDNA for each of the ten PaSABATH genes was cloned and expressed in Escherichia coli . Recombinant PaSABATHs were tested for activity with IAA, GA, SA, and JA. Among the ten PaSABATHs, five had activity with one or more of the four substrates. PaSABATH1 and PaSABATH2 had the highest activities with IAA and SA, respectively. PaSABATH4, PaSABATH5 and PaSABATH10 all had JA as a preferred substrate but with notable differences in biochemical properties. The structural basis of PaSABATHs in discriminating various phytohormone substrates was inferred based on structural models of the enzyme-substrate complexes. The phylogeny of PaSABATHs with selected SABATHs from other plants implies that the enzymes methylating IAA are conserved in seed plants whereas the enzymes methylating JA and SA have independent evolution in gymnosperms and angiosperms. Graphical abstract: The gymnosperm Norway spruce contains three jasmonic acid methyltransferase genes, which appear to have evolved independently from those in angiosperms.Image 1 Highlights: The Norway spruce 10-member SABATH family include one IAMT, one SAMT and three JAMTs . IAMTs are conserved in seed plants. JAMT evolved independently in gymnosperms and angiosperms. … (more)
- Is Part Of:
- Phytochemistry. Volume 149(2018)
- Journal:
- Phytochemistry
- Issue:
- Volume 149(2018)
- Issue Display:
- Volume 149, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 149
- Issue:
- 2018
- Issue Sort Value:
- 2018-0149-2018-0000
- Page Start:
- 146
- Page End:
- 154
- Publication Date:
- 2018-05
- Subjects:
- Picea abies -- Norway spruce -- SABATH methyltransferase -- Jasmonic acid
Botanical chemistry -- Periodicals
Biochemistry -- Periodicals
Botany -- Periodicals
Chimie végétale -- Périodiques
572.2 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00319422 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.phytochem.2018.02.010 ↗
- Languages:
- English
- ISSNs:
- 0031-9422
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6489.800000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 11592.xml