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|Title:||A relaxed specificity in interchain disulfide bond formation characterises the assembly of a low-molecular-weight glutenin subunit in the endoplasmic reticulum||Authors:||Lombardi, Alessio
Della Cristina, Pietro
Castellazzi, Chiara Lara
|Keywords:||Low molecular weight glutenin subunits;Wheat;Disulfide bonds;Cysteine residues||Issue Date:||2009||Publisher:||American Society of Plant Biologists||Source:||Lombardi A. et al. 2009. A relaxed specificity in interchain disulfide bond formation characterises the assembly of a low-molecular-weight glutenin subunit in the endoplasmic reticulum. "Plant Physiology" 149(1): 412-423||Abstract:||
Wheat (Triticum aestivum) grains contain large protein polymers constituted by two main classes of polypeptides: the highmolecular-
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.
L'articolo è disponibile sul sito dell'editore: http://www.aspb.org
|Appears in Collections:||DABAC - Archivio della produzione scientifica|
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