HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 34, 32322-32329, August 24, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/34/32322    most recent M103833200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Orsi, A. Articles by Ceriotti, A. Search for Related Content PubMed PubMed Citation Articles by Orsi, A. Articles by Ceriotti, A. Social Bookmarking                      What's this?

Role of Individual Disulfide Bonds in the Structural Maturation of a Low Molecular Weight Glutenin Subunit^*

Andrea Orsi, Francesca Sparvoli, and Aldo Ceriotti^§

From the Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, via Bassini 15, 20133 Milano, Italy

Gliadins and glutenins are the major storage proteins that accumulate in wheat endosperm cells during seed development. Although gliadins are mainly monomeric, glutenins consist of very large disulfide-linked polymers made up of high molecular weight and low molecular weight subunits. These polymers are among the largest protein molecules known in nature and are the most important determinants of the viscoelastic properties of gluten. As a first step toward the elucidation of the folding and assembly pathways that lead to glutenin polymer formation, we have exploited an in vitro system composed of wheat germ extract and bean microsomes to examine the role of disulfide bonds in the structural maturation of a low molecular weight glutenin subunit. When conditions allowing the formation of disulfide bonds were established, the in vitro synthesized low molecular weight glutenin subunit was recovered in monomeric form containing intrachain disulfide bonds. Conversely, synthesis under conditions that did not favor the formation of disulfide bonds led to the production of large aggregates from which the polypeptides could not be rescued by the post-translational generation of a more oxidizing environment. These results indicate that disulfide bond formation is essential for the conformational maturation of the low molecular weight glutenin subunit and suggest that early folding steps may play an important role in this process, allowing the timely pairing of critical cysteine residues. To determine which cysteines were important to maintain the protein in monomeric form, we prepared a set of mutants containing selected cysteine to serine substitutions. Our results show that two conserved cysteine residues form a critical disulfide bond that is essential in preventing the exposure of adhesive domains and the consequent formation of aberrant aggregates.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. Lombardi, A. Barbante, P. D. Cristina, D. Rosiello, C. L. Castellazzi, L. Sbano, S. Masci, and A. Ceriotti A Relaxed Specificity in Interchain Disulfide Bond Formation Characterizes the Assembly of a Low-Molecular-Weight Glutenin Subunit in the Endoplasmic Reticulum Plant Physiology, January 1, 2009; 149(1): 412 - 423. [Abstract] [Full Text] [PDF]

				M. Nikulina, C. Habich, S. B. Flohe, F. W. Scott, and H. Kolb Wheat Gluten Causes Dendritic Cell Maturation and Chemokine Secretion J. Immunol., August 1, 2004; 173(3): 1925 - 1933. [Abstract] [Full Text] [PDF]