Molecular Modeling of the N-terminal Regions of High Molecular Weight Glutenin Subunits 7 and 5 in Relation to Intramolecular Disulfide Bond Formation

1997 ◽  
Vol 74 (2) ◽  
pp. 154-158 ◽  
Author(s):  
Peter Köhler ◽  
Bettina Keck-Gassenmeier ◽  
Herbert Wieser ◽  
Donald D. Kasarda
Keyword(s):  
Molecular Weight ◽  
Molecular Modeling ◽  
High Molecular Weight ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Glutenin Subunits ◽  
Intramolecular Disulfide Bond

scholarly journals A Relaxed Specificity in Interchain Disulfide Bond Formation Characterizes the Assembly of a Low-Molecular-Weight Glutenin Subunit in the Endoplasmic Reticulum

2008 ◽  
Vol 149 (1) ◽  
pp. 412-423 ◽  
Author(s):  
Alessio Lombardi ◽  
Alessandra Barbante ◽  
Pietro Della Cristina ◽  
Daniele Rosiello ◽  
Chiara Lara Castellazzi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Endoplasmic Reticulum ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation ◽  
Interchain Disulfide Bond

scholarly journals Disulfide Bond Formation in Secreton Component PulK Provides a Possible Explanation for the Role of DsbA in Pullulanase Secretion

2001 ◽  
Vol 183 (4) ◽  
pp. 1312-1319 ◽  
Author(s):  
Anthony P. Pugsley ◽  
Nicolas Bayan ◽  
Nathalie Sauvonnet
Keyword(s):  
Disulfide Bond ◽  
Klebsiella Oxytoca ◽  
Bond Formation ◽  
Type Ii Secretion ◽  
Disulfide Bond Formation ◽  
Gene Encoding ◽  
Intramolecular Disulfide Bond ◽  
Disulfide Oxidoreductase ◽  
Considerable Excess

ABSTRACT When expressed in Escherichia coli, the 15Klebsiella oxytoca pul genes that encode the so-called Pul secreton or type II secretion machinery promote pullulanase secretion and the assembly of one of the secreton components, PulG, into pili. Besides these pul genes, efficient pullulanase secretion also requires the host dsbA gene, encoding a periplasmic disulfide oxidoreductase, independently of disulfide bond formation in pullulanase itself. Two secreton components, the secretin pilot protein PulS and the minor pseudopilin PulK, were each shown to posses an intramolecular disulfide bond whose formation was catalyzed by DsbA. PulS was apparently destabilized by the absence of its disulfide bond, whereas PulK stability was not dramatically affected either by adsbA mutation or by the removal of one of its cysteines. The pullulanase secretion defect in a dsbA mutant was rectified by overproduction of PulK, indicating reduced disulfide bond formation in PulK as the major cause of the secretion defect under the conditions tested (in which PulS is probably present in considerable excess of requirements). PulG pilus formation was independent of DsbA, probably because PulK is not needed for piliation.

scholarly journals On-column disulfide bond formation of monoclonal antibodies during Protein A chromatography eliminates low molecular weight species and rescues reduced antibodies

mAbs ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 1829333
Author(s):  
Zhijun Tan ◽  
Vivekh Ehamparanathan ◽  
Tingwei Ren ◽  
Peifeng Tang ◽  
Laurel Hoffman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Protein A ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation

Inhibition of Human Cytomegalovirus UL80 Protease by Specific Intramolecular Disulfide Bond Formation†

Biochemistry ◽  
1996 ◽  
Vol 35 (18) ◽  
pp. 5838-5846 ◽  
Author(s):  
Ellen Z. Baum ◽  
Marshall M. Siegel ◽  
Geraldine A. Bebernitz ◽  
Jeffrey D. Hulmes ◽  
Latha Sridharan ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Intramolecular Disulfide Bond

Charcoal surface-assisted catalysis of intramolecular disulfide bond formation in peptides

2009 ◽  
Vol 51 (5) ◽  
pp. 365-369 ◽  
Author(s):  
RUDOLF VOLKMER-ENGERT ◽  
CHRISTIANE LANDGRAF ◽  
JENS SCHNEIDER-MERGENER
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Intramolecular Disulfide Bond

Control of the toxic conformation of amyloid β42 by intramolecular disulfide bond formation

2020 ◽  
Vol 56 (29) ◽  
pp. 4118-4121 ◽  
Author(s):  
Yuka Matsushima ◽  
Ryo C. Yanagita ◽  
Kazuhiro Irie
Keyword(s):  
Amino Acid ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Amino Acid Residues ◽  
Intramolecular Disulfide Bond

An Aβ42 analog crosslinked within the molecule at the 17th and 28th amino acid residues exhibited high aggregative ability and potent neurotoxicity comparable to those of E22P-Aβ42.

scholarly journals Role of the Intramolecular Disulfide Bond in FlgI, the Flagellar P-Ring Component of Escherichia coli

2006 ◽  
Vol 188 (12) ◽  
pp. 4190-4197 ◽  
Author(s):  
Yohei Hizukuri ◽  
Toshiharu Yakushi ◽  
Ikuro Kawagishi ◽  
Michio Homma
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Self Assembly ◽  
Bacterial Species ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Wild Type ◽  
Ring Assembly ◽  
Intramolecular Disulfide Bond

ABSTRACT The P ring of the bacterial flagellar motor consists of multiple copies of FlgI, a periplasmic protein. The intramolecular disulfide bond in FlgI has previously been reported to be essential for P-ring assembly in Escherichia coli, because the P ring was not assembled in a dsbB strain that was defective for disulfide bond formation in periplasmic proteins. We, however, found that the two Cys residues of FlgI are not conserved in other bacterial species. We then assessed the role of this intramolecular disulfide bond in FlgI. A Cys-eliminated FlgI derivative formed a P ring that complemented the flagellation defect of our ΔflgI strain when it was overproduced, suggesting that disulfide bond formation in FlgI is not absolutely required for P-ring assembly. The levels of the mature forms of the FlgI derivatives were significantly lower than that of wild-type FlgI, although the precursor protein levels were unchanged. Moreover, the FlgI derivatives were more susceptible to degradation than wild-type FlgI. Overproduction of FlgI suppressed the motility defect of ΔdsbB cells. Additionally, the low level of FlgI observed in the ΔdsbB strain increased in the presence of l-cystine, an oxidative agent. We propose that intramolecular disulfide bond formation facilitates the rapid folding of the FlgI monomer to protect against degradation in the periplasmic space, thereby allowing its efficient self-assembly into the P ring.

scholarly journals Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys Peroxide Sensor

2008 ◽  
Vol 190 (17) ◽  
pp. 5738-5745 ◽  
Author(s):  
Sumarin Soonsanga ◽  
Jin-Won Lee ◽  
John D. Helmann
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Disulfide Bond ◽  
Active Sites ◽  
Xanthomonas Campestris ◽  
Bond Formation ◽  
Cysteine Residue ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation ◽  
Protein Dimer

ABSTRACTOhrR proteins can be divided into two groups based on their inactivation mechanism: 1-Cys (represented byBacillus subtilisOhrR) and 2-Cys (represented byXanthomonas campestrisOhrR). A conserved cysteine residue near the amino terminus is present in both groups of proteins and is initially oxidized to the sulfenic acid. TheB. subtilis1-Cys OhrR protein is subsequently inactivated by formation of a mixed-disulfide bond with low-molecular-weight thiols or by cysteine overoxidation to sulfinic and sulfonic acids. In contrast, theX. campestris2-Cys OhrR is inactivated when the initially oxidized cysteine sulfenate forms an intersubunit disulfide bond with a second Cys residue from the other subunit of the protein dimer. Here, we demonstrate that the 1-CysB. subtilisOhrR can be converted into a 2-Cys OhrR by introducing another cysteine residue in either position 120 or position 124. Like theX. campestrisOhrR protein, these mutants (G120C and Q124C) are inactivated by intermolecular disulfide bond formation. Analysis of oxidized 2-Cys variants both in vivo and in vitro indicates that intersubunit disulfide bond formation can occur simultaneously at both active sites in the protein dimer. Rapid formation of intersubunit disulfide bonds protects OhrR against irreversible overoxidation in the presence of strong oxidants much more efficiently than do the endogenous low-molecular-weight thiols.

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