scholarly journals Poplar Allene Oxide Synthase 1 Gene Promoter Drives Rapid and Localized Expression by Wounding

2021 ◽  
pp. 16-28
Author(s):  
Bin Lei ◽  
Christopher J. Frost ◽  
Tao Xu ◽  
Joshua R. Herr ◽  
John E. Carlson ◽  
...  
Keyword(s):  
Expression Patterns ◽  
Regulation Of Gene Expression ◽  
Gene Promoter ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Lipoxygenase Pathway ◽  
Binding Motifs ◽  
Inducible Promoters ◽  
Essential Enzyme ◽  
Oxide Synthase

Promoters play critical roles in controlling the transcription of genes and are important as tools to drive heterologous expression for biotechnological applications. In addition to core transcription factor-binding motifs that assist in the binding of RNA polymerases, there are specific nucleotide sequences in a promoter region to allow regulation of gene expression. The allene oxide synthase (AOS) gene family are cytochrome P450s that are responsive to a variety of environmental stress, making them good candidates for the discovery of inducible promoters. Populus AOS homologs separate phylogenetically into two clades. Based on the 19 promoter motifs with significant abundance differences between the two clades, Clade I AOS genes are likely more responsive to hormones, salt, and pathogen, whereas clade II homologs are likely inducible by water stress. In this study, an upstream promoter from a Clade I poplar AOS encoding gene (AOS1) was cloned and used to drive the expression of a ß-glucuronidase (GUS) gene in Arabidopsis. AOS is an essential enzyme in the lipoxygenase pathway that is responsible for the production of many non-volatile oxylipins in plants, including the jasmonates, which are regulatory phytohormones coordinating a variety of biological and stress response functions. Consistent with AOS transcript expression patterns, we found that the poplar AOS1 promoter drives rapid and localized expression by wounding. The study provides insight on the responsive elements in the poplar AOS promoters, but more importantly identifies a strong wound-inducible and localized promoter for future applications.

scholarly journals The lipoxygenase pathway in tulip (Tulipa gesneriana): detection of the ketol route

2000 ◽  
Vol 352 (2) ◽  
pp. 501-509 ◽  
Author(s):  
Alexander N. GRECHKIN ◽  
Lucia S. MUKHTAROVA ◽  
Mats HAMBERG
Keyword(s):  
Octadecadienoic Acid ◽  
Optical Purity ◽  
Cyclase Activity ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Lipoxygenase Pathway ◽  
Tulipa Gesneriana ◽  
Tulip Bulbs ◽  
Oxide Synthase

The in vitro metabolism of [1-14C]linoleate, [1-14C]linolenate and their 9(S)-hydroperoxides was studied in cell-free preparations from tulip (Tulipa gesneriana) bulbs, leaves and flowers. Linoleate and its 9-hydroperoxide were converted by bulb and leaf preparations into three ketols: (12Z)-9-hydroxy-10-oxo-12-octadecadienoic acid (α-ketol), (11E)-10-oxo-13-hydroxy-11-octadecadienoic acid (γ-ketol) and a novel compound, (12Z)-10-oxo-11-hydroxy-12-octadecadienoic acid (10,11-ketol), in the approximate molar proportions of 10:3:1. The corresponding 15,16-dehydro α- and γ-ketols were the main metabolites of [1-14C]linolenate and its 9-hydroperoxide. Thus bulbs and leaves possessed 9-lipoxygenase and allene oxide synthase activities. Incubations with flower preparations gave α-ketol hydro(pero)xides as predominant metabolites. Bulb and leaf preparations possessed a novel enzyme activity, γ-ketol reductase, which reduces γ-ketol to 10-oxo-13-hydroxyoctadecanoic acid (dihydro-γ-ketol) in the presence of NADH. Exogenous linolenate 13(S)-hydroperoxide was converted mostly into chiral (9S,13S)-12-oxo-10-phytodienoate (99.5% optical purity) by bulb preparations, while [1-14C]linolenate was a precursor for ketols only. Thus tulip bulbs possess abundant allene oxide cyclase activity, the substrate for which is linolenate 13(S)-hydroperoxide, even though 13(S)-lipoxygenase products were not detectable in the bulbs. The majority of the cyclase activity was found in the microsomes (105g pellet). Cyclase activity was not found in the other tissues examined, but only in the bulbs. The ketol route of the lipoxygenase pathway, mediated by 9-lipoxygenase and allene oxide synthase activities, has not been detected previously in the vegetative organs of any plant species.

Lipoxygenase pathway in tulip: biosynthesis of ketols

2000 ◽  
Vol 28 (6) ◽  
pp. 851-853 ◽  
Author(s):  
A. N. Grechkin ◽  
L. S. Mukhtarova ◽  
M. Hamberg
Keyword(s):  
Octadecadienoic Acid ◽  
Allene Oxide ◽  
The Novel ◽  
Allene Oxide Synthase ◽  
Allene Oxide Cyclase ◽  
Lipoxygenase Pathway ◽  
Tulipa Gesneriana ◽  
Oxide Synthase

The metabolism in vitro of [1-14C]linoleate, [1-14C]linolenate and their 9(S)-hydroperoxides in tulip (Tulipa gesneriana) was found to be under the control of 9-lipoxygenase and allene oxide synthase, and directed towards α-ketol, γ-ketol and the novel compound (12Z)-10-oxo-11-hydroxy- 12-octadecadienoic acid (10,11-ketol). Potent activity of allene oxide cyclase (in bulbs) and a new enzyme, γ-ketol reductase (in bulbs and leaves), was detected. Metabolism in flowers is directed predominantly towards α-ketol hydroperoxide.

scholarly journals Wounding stimulates ALLENE OXIDE SYNTHASE gene and increases the level of jasmonic acid in Ipomoea nil cotyledons

2016 ◽  
Vol 85 (1) ◽  
Author(s):  
Emilia Wilmowicz ◽  
Agata Kućko ◽  
Kamil Frankowski ◽  
Barbara Zabrocka-Nowakowska ◽  
Katarzyna Panek ◽  
...  
Keyword(s):  
Jasmonic Acid ◽  
Stress Responses ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Lipoxygenase Pathway ◽  
Ipomoea Nil ◽  
Evolutionarily Conserved ◽  
Strong Stimulation ◽  
Oxide Synthase

<em>Allene oxide synthase</em> (<em>AOS</em>) encodes the first enzyme in the lipoxygenase pathway, which is responsible for jasmonic acid (JA) formation. In this study we report the molecular cloning and characterization of <em>InAOS</em> from <em>Ipomoea nil</em>. The full-length gene is composed of 1662 bp and encodes for 519 amino acids. The predicted InAOS contains PLN02648 motif, which is evolutionarily conserved and characteristic for functional enzymatic proteins. We have shown that wounding led to a strong stimulation of the examined gene activity in cotyledons and an increase in JA level, which suggest that this compound may be a modulator of stress responses in <em>I. nil</em>.

scholarly journals Specific Adduction of Plant Lipid Transfer Protein by an Allene Oxide Generated by 9-Lipoxygenase and Allene Oxide Synthase

2006 ◽  
Vol 281 (51) ◽  
pp. 38981-38988 ◽  
Author(s):  
Bénédicte Bakan ◽  
Mats Hamberg ◽  
Ludivine Perrocheau ◽  
Daniel Maume ◽  
Hélène Rogniaux ◽  
...  
Keyword(s):  
Lipid Transfer Protein ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Lipid Transfer ◽  
Plant Lipid ◽  
Transfer Protein ◽  
Oxide Synthase

scholarly journals Functional Characterization of An Allene Oxide Synthase Involved in Biosynthesis of Jasmonic Acid and Its Influence on Metabolite Profiles and Ethylene Formation in Tea (Camellia sinensis) Flowers

2018 ◽  
Vol 19 (8) ◽  
pp. 2440 ◽  
Author(s):  
Qiyuan Peng ◽  
Ying Zhou ◽  
Yinyin Liao ◽  
Lanting Zeng ◽  
Xinlan Xu ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Jasmonic Acid ◽  
Camellia Sinensis ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Tea Leaves ◽  
Ethylene Formation ◽  
Horticultural Crops ◽  
Metabolite Profiles ◽  
Oxide Synthase

Jasmonic acid (JA) is reportedly involved in the interaction between insects and the vegetative parts of horticultural crops; less attention has, however, been paid to its involvement in the interaction between insects and the floral parts of horticultural crops. Previously, we investigated the allene oxide synthase 2 (AOS2) gene that was found to be the only JA synthesis gene upregulated in tea (Camellia sinensis) flowers exposed to insect (Thrips hawaiiensis (Morgan)) attacks. In our present study, transient expression analysis in Nicotiana benthamiana plants confirmed that CsAOS2 functioned in JA synthesis and was located in the chloroplast membrane. In contrast to tea leaves, the metabolite profiles of tea flowers were not significantly affected by 10 h JA (2.5 mM) treatment as determined using ultra-performance liquid chromatography/quadrupole time-of-flight mass spectrometry, and gas chromatography-mass spectrometry. Moreover, JA treatment did not significantly influence ethylene formation in tea flowers. These results suggest that JA in tea flowers may have different functions from JA in tea leaves and other flowers.

scholarly journals Jasmonates: what ALLENE OXIDE SYNTHASE does for plants

2019 ◽  
Vol 70 (13) ◽  
pp. 3373-3378 ◽  
Author(s):  
Edward E Farmer ◽  
Alain Goossens
Keyword(s):  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Oxide Synthase

Allene oxide synthase and hydroperoxide lyase product accumulation in Artemisia species

Plant Science ◽  
2005 ◽  
Vol 169 (1) ◽  
pp. 139-146 ◽  
Author(s):  
Meshack Afitlhile ◽  
Hirotada Fukushige ◽  
Charles McCraken ◽  
David Hildebrand
Keyword(s):  
Hydroperoxide Lyase ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Artemisia Species ◽  
Oxide Synthase ◽  
Product Accumulation

scholarly journals ALLENE OXIDE SYNTHASE and HYDROPEROXIDE LYASE, Two Non-Canonical Cytochrome P450s in Arabidopsis thaliana and Their Different Roles in Plant Defense

2019 ◽  
Vol 20 (12) ◽  
pp. 3064 ◽  
Author(s):  
Sachin Rustgi ◽  
Armin Springer ◽  
ChulHee Kang ◽  
Diter von Wettstein ◽  
Christiane Reinbothe ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Plant Defense ◽  
Metabolic Regulation ◽  
Insect Pests ◽  
Green Leaf Volatiles ◽  
Hydroperoxide Lyase ◽  
Allene Oxide ◽  
Allene Oxide Synthase ◽  
Cytochrome P450 Enzymes ◽  
Oxide Synthase

The channeling of metabolites is an essential step of metabolic regulation in all living organisms. Multifunctional enzymes with defined domains for metabolite compartmentalization are rare, but in many cases, larger assemblies forming multimeric protein complexes operate in defined metabolic shunts. In Arabidopsis thaliana, a multimeric complex was discovered that contains a 13-lipoxygenase and allene oxide synthase (AOS) as well as allene oxide cyclase. All three plant enzymes are localized in chloroplasts, contributing to the biosynthesis of jasmonic acid (JA). JA and its derivatives act as ubiquitous plant defense regulators in responses to both biotic and abiotic stresses. AOS belongs to the superfamily of cytochrome P450 enzymes and is named CYP74A. Another CYP450 in chloroplasts, hydroperoxide lyase (HPL, CYP74B), competes with AOS for the common substrate. The products of the HPL reaction are green leaf volatiles that are involved in the deterrence of insect pests. Both enzymes represent non-canonical CYP450 family members, as they do not depend on O2 and NADPH-dependent CYP450 reductase activities. AOS and HPL activities are crucial for plants to respond to different biotic foes. In this mini-review, we aim to summarize how plants make use of the LOX2–AOS–AOC2 complex in chloroplasts to boost JA biosynthesis over volatile production and how this situation may change in plant communities during mass ingestion by insect pests.

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