Universität zu Köln

Nakano, Ryohei T., Pislewska-Bednarek, Mariola ORCID: 0000-0001-9241-3328, Yamada, Kenji ORCID: 0000-0003-4872-3729, Edger, Patrick P., Miyahara, Mado, Kondo, Maki, Boettcher, Christoph, Mori, Masashi, Nishimura, Mikio, Schulze-Lefert, Paul, Hara-Nishimura, Ikuko and Bednarek, Pawel ORCID: 0000-0002-3064-7775 (2017). PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in Arabidopsis thaliana. Plant J., 89 (2). S. 204 - 221. HOBOKEN: WILEY. ISSN 1365-313X

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Abstract

The endoplasmic reticulum body (ER body) is an organelle derived from the ER that occurs in only three families of the order Brassicales and is suggested to be involved in plant defense. ER bodies in Arabidopsis thaliana contain large amounts of b-glucosidases, but the physiological functions of ER bodies and these enzymes remain largely unclear. Here we show that PYK10, the most abundant b-glucosidase in A. thaliana root ER bodies, hydrolyzes indole glucosinolates (IGs) in addition to the previously reported in vitro substrate scopolin. We found a striking co-expression between ER body-related genes (including PYK10), glucosinolate biosynthetic genes and the genes for so-called specifier proteins affecting the terminal products of myrosinase-mediated glucosinolate metabolism, indicating that these systems have been integrated into a common transcriptional network. Consistent with this, comparative metabolite profiling utilizing a number of A. thaliana relatives within Brassicaceae identified a clear phylogenetic co-occurrence between ER bodies and IGs, but not between ER bodies and scopolin. Collectively, our findings suggest a functional link between ER bodies and glucosinolate metabolism in planta. In addition, in silico three-dimensional modeling, combined with phylogenomic analysis, suggests that PYK10 represents a clade of 16 myrosinases that arose independently from the other well-documented class of six thioglucoside glucohydrolases. These findings provide deeper insights into how glucosinolates are metabolized in cruciferous plants and reveal variation of the myrosinase-glucosinolate system within individual plants.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Nakano, Ryohei T. UNSPECIFIED UNSPECIFIED UNSPECIFIED Pislewska-Bednarek, Mariola UNSPECIFIED orcid.org/0000-0001-9241-3328 UNSPECIFIED Yamada, Kenji UNSPECIFIED orcid.org/0000-0003-4872-3729 UNSPECIFIED Edger, Patrick P. UNSPECIFIED UNSPECIFIED UNSPECIFIED Miyahara, Mado UNSPECIFIED UNSPECIFIED UNSPECIFIED Kondo, Maki UNSPECIFIED UNSPECIFIED UNSPECIFIED Boettcher, Christoph UNSPECIFIED UNSPECIFIED UNSPECIFIED Mori, Masashi UNSPECIFIED UNSPECIFIED UNSPECIFIED Nishimura, Mikio UNSPECIFIED UNSPECIFIED UNSPECIFIED Schulze-Lefert, Paul UNSPECIFIED UNSPECIFIED UNSPECIFIED Hara-Nishimura, Ikuko UNSPECIFIED UNSPECIFIED UNSPECIFIED Bednarek, Pawel UNSPECIFIED orcid.org/0000-0002-3064-7775 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-243921
DOI:	10.1111/tpj.13377
Journal or Publication Title:	Plant J.
Volume:	89
Number:	2
Page Range:	S. 204 - 221
Date:	2017
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1365-313X
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language INDUCED SYSTEMIC RESISTANCE; MYB TRANSCRIPTION FACTORS; BETA-GLUCOSIDASE; ER BODY; DILATED CISTERNAE; SECONDARY METABOLITES; PHYLOGENETIC TREES; NONHOST RESISTANCE; GENE COEXPRESSION; IRON-DEFICIENCY Multiple languages Plant Sciences Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/24392