We are analyzing https://link.springer.com/article/10.1007/s00425-009-1080-6.

Title:
A tomato enzyme synthesizes (+)-7-iso-jasmonoyl-l-isoleucine in wounded leaves | Planta
Description:
Jasmonoyl-l-isoleucine (JA-Ile) is a key jasmonate signal that probably functions in all plant species. The JASMONATE RESISTANT 1 (JAR1) enzyme synthesizes JA-Ile in Arabidopsis [Arabidopsis thaliana (L.) Heynh.], but a similar enzyme from tomato [Solanum lycopersicum (L.)] was not previously described. Tomato SlJAR1 has 66% sequence identity with Arabidopsis JAR1 and the SlJAR1-GST fusion protein purified from Escherichia coli catalyzed the formation of JA-amino acid conjugates in vitro. Kinetic analysis showed the enzyme has a strong preference for Ile over Leu and Val and it was about 10-fold more active with (+)-7-iso-JA than with its epimer (−)-JA. Leaf wounding rapidly increased JA-Ile 50-fold to about 450 pmol g−1 FW at 30 min after wounding, while conjugates with Leu, Phe, Val and Met were only marginally increased or not detected. Nearly all of the endogenous JA-Ile was the bioactive epimer (+)-7-iso-JA-Ile and there was no evidence for its conversion to (−)-JA-Ile up to 6 h after wounding. A transgenic RNAi approach was used to suppress SlJAR1 transcript that reduced JA-Ile accumulation by 50–75%, suggesting that other JA conjugating enzymes may be present. These results show that SlJAR1 synthesizes the bioactive conjugate (+)-7-iso-JA-Ile and this is the predominant isomer accumulated in wounded tomato leaves.
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Keywords {🔍}

article, cas, google, scholar, pubmed, plant, jasmonate, tomato, arabidopsis, howe, signaling, staswick, acid, cell, biol, jar, response, usa, enzyme, jasmonic, defense, sci, signal, systemic, wound, leaves, suza, jaile, access, jaz, ryan, proc, natl, acad, annu, rev, mutant, privacy, cookies, content, analysis, research, planta, rowe, wounding, physiol, wang, university, publish, search,

Topics {✒️}

acyl-adenylate/thioester-forming enzyme superfamily month download article/chapter 7-iso-jasmonoyl-l-isoleucine jasmonoyl-l-isoleucine production cdna-deduced primary structure wound-induced proteinase inhibitors tissue-specific oxylipin signature site-directed mutagenesis study reduced ja-ile accumulation ja-amino acid conjugates ja conjugating enzymes jasmonate-signaled defense responses coi1-dependent jasmonate pathway auxin-signaling mutant axr1 enzyme synthesizes ja-ile acyl-adenylate motif full article pdf amino acid synthetase jaz repressor proteins indole-3-acetic acid jasmonic acid privacy choices/manage cookies article planta aims pre-inhibitor ii molecular actions firefly luciferase superfamily systemic wound signal trypsin proteinase inhibitors octadecanoid pathway mutant wounded tomato leaves systemic wound signaling systemic wound response plant hormone binding 7-iso-ja-ile plant stress response systemin activates synthesis plant hormone jasmonate tomato [solanum lycopersicum tomato mutant spr1 endogenous ja-ile tomato enzyme synthesizes arabidopsis wound response european economic area escherichia coli catalyzed transgenic rnai approach suppress sljar1 transcript predominant isomer accumulated strain cbs3 4-chlorobenzoate koo aj signal propagation leading

Schema {🗺️}

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         description:Jasmonoyl-l-isoleucine (JA-Ile) is a key jasmonate signal that probably functions in all plant species. The JASMONATE RESISTANT 1 (JAR1) enzyme synthesizes JA-Ile in Arabidopsis [Arabidopsis thaliana (L.) Heynh.], but a similar enzyme from tomato [Solanum lycopersicum (L.)] was not previously described. Tomato SlJAR1 has 66% sequence identity with Arabidopsis JAR1 and the SlJAR1-GST fusion protein purified from Escherichia coli catalyzed the formation of JA-amino acid conjugates in vitro. Kinetic analysis showed the enzyme has a strong preference for Ile over Leu and Val and it was about 10-fold more active with (+)-7-iso-JA than with its epimer (−)-JA. Leaf wounding rapidly increased JA-Ile 50-fold to about 450 pmol g−1 FW at 30 min after wounding, while conjugates with Leu, Phe, Val and Met were only marginally increased or not detected. Nearly all of the endogenous JA-Ile was the bioactive epimer (+)-7-iso-JA-Ile and there was no evidence for its conversion to (−)-JA-Ile up to 6 h after wounding. A transgenic RNAi approach was used to suppress SlJAR1 transcript that reduced JA-Ile accumulation by 50–75%, suggesting that other JA conjugating enzymes may be present. These results show that SlJAR1 synthesizes the bioactive conjugate (+)-7-iso-JA-Ile and this is the predominant isomer accumulated in wounded tomato leaves.
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      description:Jasmonoyl-l-isoleucine (JA-Ile) is a key jasmonate signal that probably functions in all plant species. The JASMONATE RESISTANT 1 (JAR1) enzyme synthesizes JA-Ile in Arabidopsis [Arabidopsis thaliana (L.) Heynh.], but a similar enzyme from tomato [Solanum lycopersicum (L.)] was not previously described. Tomato SlJAR1 has 66% sequence identity with Arabidopsis JAR1 and the SlJAR1-GST fusion protein purified from Escherichia coli catalyzed the formation of JA-amino acid conjugates in vitro. Kinetic analysis showed the enzyme has a strong preference for Ile over Leu and Val and it was about 10-fold more active with (+)-7-iso-JA than with its epimer (−)-JA. Leaf wounding rapidly increased JA-Ile 50-fold to about 450 pmol g−1 FW at 30 min after wounding, while conjugates with Leu, Phe, Val and Met were only marginally increased or not detected. Nearly all of the endogenous JA-Ile was the bioactive epimer (+)-7-iso-JA-Ile and there was no evidence for its conversion to (−)-JA-Ile up to 6 h after wounding. A transgenic RNAi approach was used to suppress SlJAR1 transcript that reduced JA-Ile accumulation by 50–75%, suggesting that other JA conjugating enzymes may be present. These results show that SlJAR1 synthesizes the bioactive conjugate (+)-7-iso-JA-Ile and this is the predominant isomer accumulated in wounded tomato leaves.
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