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Glucosinolate hydrolysis in Lepidium sativum--identification of the thiocyanate-forming protein.

Abstract：

:Glucosinolates are a class of thioglycosides found predominantly in plants of the order Brassicales whose function in anti-herbivore defense has been attributed to the products formed by myrosinase-catalyzed hydrolysis upon plant tissue damage. The most common type of hydrolysis products, the isothiocyanates, are toxic to a wide range of organisms. Depending on the glucosinolate side-chain structure and the presence of certain protein factors, other types of hydrolysis products, such as simple nitriles, epithionitriles and organic thiocyanates, can be formed whose biological functions are not well understood. Of the proteins controlling glucosinolate hydrolysis, only epithiospecifier proteins (ESPs) that promote the formation of simple nitriles and epithionitriles have been identified on a molecular level. We investigated glucosinolate hydrolysis in Lepidium sativum and identified a thiocyanate-forming protein (TFP) that shares 63-68% amino acid sequence identity with known ESPs and up to 55% identity with myrosinase-binding proteins from Arabidopsis thaliana, but differs from ESPs in its biochemistry. TFP does not only catalyze thiocyanate and simple nitrile formation from benzylglucosinolate but also the formation of simple nitriles and epithionitriles from aliphatic glucosinolates. Analyses of glucosinolate hydrolysis products in L. sativum autolysates and TFP transcript accumulation revealed an organ-specific regulation of thiocyanate formation. The identification of TFP defines a new family of proteins that control glucosinolate hydrolysis and challenges the previously proposed reaction mechanism of epithionitrile formation. As a protein that promotes the formation of a wide variety of hydrolysis products, its identification provides an important tool for further elucidating the mechanisms of glucosinolate hydrolysis as well as the ecological role and the evolutionary origin of the glucosinolate-myrosinase system.

journal_name

Plant Mol Biol

journal_title

Plant molecular biology

authors

Burow M,Bergner A,Gershenzon J,Wittstock U

doi

10.1007/s11103-006-9071-5

subject

Has Abstract

pub_date

2007-01-01 00:00:00

pages

49-61

issue

1

eissn

0167-4412

issn

1573-5028

journal_volume

63

pub_type

杂志文章

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