2011
DOI: 10.1016/j.bbrc.2011.05.055
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OsJAR1 and OsJAR2 are jasmonyl-l-isoleucine synthases involved in wound- and pathogen-induced jasmonic acid signalling

Abstract: The synthesis of JA-Ile was catalysed by JA-Ile synthase, which is a member of the group I GH3 family of proteins. Here, we showed evidence that OsGH3.5 (OsJAR1) and OsGH3.3 (OsJAR2) are the functional JA-Ile synthases in rice, using recombinant proteins. The expression levels of OsJAR1 and OsJAR2 were induced in response to wounding with the concomitant accumulation of JA-Ile. In contrast, only the expression of OsJAR1 was associated with the accumulation of JA-Ile after blast infection. Our data suggest that… Show more

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Cited by 72 publications
(64 citation statements)
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“…Very recently, a Japanese group demonstrated that in fact two enzymes, OsJAR1 and OsGH3.3 (called OsJAR2 hereafter) are able to conjugate JA to Ile in crude extracts of Escherichia coli expressing the respective proteins (Wakuta et al 2011). Our own in vitro experiments using recombinant purified GST-tagged enzymes confirm this result, and additionally demonstrate that multiple amino acids can be used as a substrate by both enzymes (Svyatyna et al, manuscript in preparation).…”
Section: Photomorphogenic Responses Require Several Gh3 Enzymes In Ricesupporting
confidence: 64%
“…Very recently, a Japanese group demonstrated that in fact two enzymes, OsJAR1 and OsGH3.3 (called OsJAR2 hereafter) are able to conjugate JA to Ile in crude extracts of Escherichia coli expressing the respective proteins (Wakuta et al 2011). Our own in vitro experiments using recombinant purified GST-tagged enzymes confirm this result, and additionally demonstrate that multiple amino acids can be used as a substrate by both enzymes (Svyatyna et al, manuscript in preparation).…”
Section: Photomorphogenic Responses Require Several Gh3 Enzymes In Ricesupporting
confidence: 64%
“…Also, overexpression of rice OPR7 in Arabidopsis complemented opr3 defects, indicating rice OPR7 is a JAproducing enzyme (Tani et al, 2008). Moreover, recombinant JAR1 and JAR2 proteins showed JA-Ile-conjugating activity, and JAR1 and JAR2 are differentially induced upon wounding or pathogen challenge (Wakuta et al, 2011).…”
Section: Introductionmentioning
confidence: 92%
“…In Arabidopsis , only one protein, AtJAR1 was shown to utilize JA as a substrate [99]. In rice, two proteins were shown to produce JA-Ile in vitro, OsJAR1 and OsJAR2 [100]. The maize genome encodes five JAR1-like isoforms that group into two clusters (Figure 9).…”
Section: Ja-amino Acid Conjugationmentioning
confidence: 99%