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GrainGenes Reference Report: PPS-135-2230

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Reference	PPS-135-2230
Title	A novel auxin conjugate hydrolase from wheat with substrate specificity for longer side-chain auxin amide conjugates
Journal	Plant Physiology
Year	2004
Volume	135
Pages	2230-2240
Author	Campanella JJ Olajide AF Magnus V Ludwig-Muller J
Abstract	This study investigates how the ILR1-like indole acetic acid (IAA) amidohydrolase family of genes has functionally evolved in the monocotyledonous species wheat (Triticum aestivum). An ortholog for the Arabidopsis IAR3 auxin amidohydrolase gene has been isolated from wheat (TaIAR3). The TaIAR3 protein hydrolyzes negligible levels of IAA-Ala and no other IAA amino acid conjugates tested, unlike its ortholog IAR3. Instead, TaIAR3 has low specificity for the ester conjugates IAA-Glc and IAA-myoinositol and high specificity for the conjugates of indole-3-butyric acid (IBA-Ala and IBA-Gly) and indole-3-propionic-acid (IPA-Ala) so far tested. TaIAR3 did not convert the methyl esters of the IBA conjugates with Ala and Gly. IBA and IBA conjugates were detected in wheat seedlings by gas chromatography-mass spectrometry, where the conjugate of IBA with Ala may serve as a natural substrate for this enzyme. Endogenous IPA and IPA conjugates were not detected in the seedlings. Additionally, crude protein extracts of wheat seedlings possess auxin amidohydrolase activity. Temporal expression studies of TaIAR3 indicate that the transcript is initially expressed at day 1 after germination. Expression decreases through days 2, 5, 10, 15, and 20. Spatial expression studies found similar levels of expression throughout all wheat tissues examined
External Databases	Pubmed: 15299127
Keyword	[ Hide all but 1 of 24 ] acetic acid amino acid arabidopsis arabidopsis thaliana chromatography mass spectrometry enzyme esters expression pattern family gene germination indole-3-butyric acid indoleacetic acid indolebutyric acid liquid chromatography methyl protein quantitative analysis root formation seedling specificity tissue triticum zea mays

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