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A relaxed specificity in interchain disulfide bond formation characterizes the assembly of a low-molecular-weight glutenin bubunit in the endoplasmic reticulum

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Lombardi, Alessio, Barbante, Alessandra, Della Cristina, Pietro, Rosiello, Daniele, Castellazzi, Chiara Lara, Sbano, L., Masci, Stefania and Ceriotti, Aldo. (2009) A relaxed specificity in interchain disulfide bond formation characterizes the assembly of a low-molecular-weight glutenin bubunit in the endoplasmic reticulum. Plant Physiology, Vol.149 (No.1). pp. 412-423. ISSN 0032-0889

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Official URL: http://dx.doi.org/10.1104/pp.108.127761

Abstract

Wheat (Triticum spp.) grains contain large protein polymers constituted by two main classes of polypeptides: the high-molecular-weight glutenin subunits and the low-molecular-weight glutenin subunits (LMW-GS). These polymers are among the largest protein molecules known in nature and are the main determinants of the superior technological properties of wheat flours. However, little is known about the mechanisms controlling the assembly of the different subunits and the way they are arranged in the final polymer. Here, we have addressed these issues by analyzing the formation of interchain disulfide bonds between identical and different LMW-GS and by studying the assembly of mutants lacking individual intrachain disulfides. Our results indicate that individual cysteine residues that remain available for disulfide bond formation in the folded monomer can form interchain disulfide bonds with a variety of different cysteine residues present in a companion subunit. These results imply that the coordinated expression of many different LMW-GS in wheat endosperm cells can potentially lead to the formation of a large set of distinct polymeric structures, in which subunits can be arranged in different configurations. In addition, we show that not all intrachain disulfide bonds are necessary for the generation of an assembly-competent structure and that the retention of a LMW-GS in the early secretory pathway is not dependent on polymer formation.

Item Type: Journal Article
Subjects: S Agriculture > SB Plant culture
Divisions: Faculty of Science > Mathematics
Journal or Publication Title: Plant Physiology
Publisher: American Society of Plant Biologists
ISSN: 0032-0889
Date: January 2009
Volume: Vol.149
Number: No.1
Number of Pages: 12
Page Range: pp. 412-423
Identification Number: 10.1104/pp.108.127761
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Funder: MIUR-FIRB, MIUR-FAR
URI: http://wrap.warwick.ac.uk/id/eprint/28698

Data sourced from Thomson Reuters' Web of Knowledge

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