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Identification of a β-glucosidase hydrolyzing tuberonic acid glucoside in rice (Oryza sativa L.)

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Title: Identification of a β-glucosidase hydrolyzing tuberonic acid glucoside in rice (Oryza sativa L.)
Authors: Wakuta, Shinji Browse this author
Hamada, Shigeki Browse this author
Ito, Hiroyuki Browse this author
Matsuura, Hideyuki Browse this author
Nabeta, Kensuke Browse this author
Matsui, Hirokazu Browse this author
Keywords: Oryza sativa L. cv. Kitaake
Gramineae
Glycoprotein
β-glucosidase
Tuberonic acid glucoside
Tuberonic acid
Enzyme purification
Issue Date: Aug-2010
Publisher: Elsevier
Journal Title: Phytochemistry
Volume: 71
Issue: 11-12
Start Page: 1280
End Page: 1288
Publisher DOI: 10.1016/j.phytochem.2010.04.025
PMID: 20570296
Abstract: Tuberonic acid (TA) and its glucoside (TAG) have been isolated from potato (Solanum tuberosum L) leaflets and shown to exhibit tuber-inducing properties. These compounds were reported to be biosynthesized from jasmonic acid (JA) by hydroxylation and subsequent glycosylation, and to be contained in various plant species. Here we describe the in vivo hydrolytic activity of TAG in rice. In this study, the TA resulting from TAG was not converted into JA. Tuberonic acid glucoside (TAG)-hydrolyzing β-glucosidase, designated OsTAGG1, was purified from rice by six purification steps with an similar to 4300-fold purification. The purified enzyme migrated as a single band on native PAGE, but as two bands with 4300-fold purification. The purified enzyme migrated as a single band on native PAGE, but as two bands with molecular masses of 42 and 26 kDa on SDS-PAGE. The results from N-terminal sequencing and peptide mass fingerprinting of both polypeptides suggested that the two bands were derived from a single polypeptide, which is a member of glycosyl hydrolase family 1. In the native enzyme, the Km and Vmax values of TAG were 31.7 μM and and 14.7 μmol/min/mg, respectively. OsTAGG1 preferentially hydrolyzed TAG and methyl TAG. Here we report that OsTAGG1 is a specific β-glucosidase hydrolyzing TAG, which releases physiologically active TA.
Type: article (author version)
URI: http://hdl.handle.net/2115/43767
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 和久田 真司

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