Consequence of the Removal of Evolutionary Conserved Disulfide Bridges on the Structure and Function of Charybdotoxin and Evidence That Particular Cysteine Spacings Govern Specific Disulfide Bond Formation

Biochemistry ◽  
1998 ◽  
Vol 37 (5) ◽  
pp. 1292-1301 ◽  
Author(s):  
Eugenia Drakopoulou ◽  
Jean Vizzavona ◽  
Jacques Neyton ◽  
Vincent Aniort ◽  
Françoise Bouet ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Structure And Function ◽  
Disulfide Bond Formation ◽  
Disulfide Bridges ◽  
And Function

scholarly journals Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function

2015 ◽  
Vol 25 (3) ◽  
pp. 572-586 ◽  
Author(s):  
Mikko Laitaoja ◽  
Helena Tossavainen ◽  
Tero Pihlajamaa ◽  
Jarkko Valjakka ◽  
Keijo Viiri ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Structure And Function ◽  
Disulfide Bond Formation ◽  
And Function

A Secreted Disulfide Catalyst Controls Extracellular Matrix Composition and Function

Science ◽  
2013 ◽  
Vol 341 (6141) ◽  
pp. 74-76 ◽  
Author(s):  
Tal Ilani ◽  
Assaf Alon ◽  
Iris Grossman ◽  
Ben Horowitz ◽  
Elena Kartvelishvily ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Disulfide Bond ◽  
De Novo ◽  
Bond Formation ◽  
Supporting Cell ◽  
Matrix Composition ◽  
Secretory Proteins ◽  
Disulfide Bond Formation ◽  
Enzyme Families ◽  
And Function

Disulfide bond formation in secretory proteins occurs primarily in the endoplasmic reticulum (ER), where multiple enzyme families catalyze cysteine cross-linking. Quiescin sulfhydryl oxidase 1 (QSOX1) is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells. We examined the physiological function for extracellular catalysis of de novo disulfide bond formation by QSOX1. QSOX1 activity was required for incorporation of laminin into the extracellular matrix (ECM) synthesized by fibroblasts, and ECM produced without QSOX1 was defective in supporting cell-matrix adhesion. We developed an inhibitory monoclonal antibody against QSOX1 that could modulate ECM properties and undermine cell migration.

scholarly journals Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway

Cells ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1994 ◽  
Author(s):  
Philip J. Robinson ◽  
Neil J. Bulleid
Keyword(s):  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Secretory Pathway ◽  
Bond Formation ◽  
Complex Problem ◽  
Structure Stability ◽  
Disulfide Bond Formation ◽  
Polypeptide Folding ◽  
Domains Of Life ◽  
And Function

Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER). How cysteines correctly pair during polypeptide folding to form the native disulfide bond pattern is a complex problem that is not fully understood. In this paper, the evidence for different folding mechanisms involved in ER-localised disulfide bond formation is reviewed with emphasis on events that occur during ER entry. Disulfide formation in nascent polypeptides is discussed with focus on (i) its mechanistic relationship with conformational folding, (ii) evidence for its occurrence at the co-translational stage during ER entry, and (iii) the role of protein disulfide isomerase (PDI) family members. This review highlights the complex array of cellular processes that influence disulfide bond formation and identifies key questions that need to be addressed to further understand this fundamental process.

scholarly journals Functional studies of per os infectivity factor 3 of Helicoverpa armigera nucleopolyhedrovirus

2012 ◽  
Vol 93 (2) ◽  
pp. 374-382 ◽  
Author(s):  
Jingjiao Song ◽  
Manli Wang ◽  
Huachao Huang ◽  
Xin Luo ◽  
Fei Deng ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Helicoverpa Armigera ◽  
Disulfide Bonds ◽  
Bond Formation ◽  
Terminal Region ◽  
Disulfide Bond Formation ◽  
Functional Studies ◽  
Nuclear Ring ◽  
Helicoverpa Armígera ◽  
And Function

PIF3 is one of the six conserved per os infectivity factors (PIFs) of baculoviruses. In this study, PIF3 of Helicoverpa armigera nucleopolyhedrovirus (HearNPV) was analysed by infectivity bioassays using a series of recombinant viruses harbouring various PIF3 truncation/substitution mutants. The results demonstrated that the N-terminal region (L26–Y45) and C-terminal region (T160–Q199) are essential for HearNPV oral infectivity. In the C-terminal T160–Q199 region, there are three conserved cysteines (C162, C164 and C185). Our results showed that substitutions of C162 or C164, predicted to be involved in disulfide-bond formation, led to a severe decrease in HearNPV per os infectivity. Mutation of C185, predicted not to be involved in disulfide-bond formation, did not affect the per os infectivity. The data suggest that disulfide bonds are important for PIF3 conformation and function. Immunofluorescence assays showed that none of the mutations affected the subcellular localization of PIF3 to the nuclear ring zone region of infected cells. Western blot results showed that all mutants except C162G and C185G failed to incorporate PIF3 into occlusion-derived viruses, which resulted in impaired oral infectivity of the latter. The data provide insights for future study of PIF3 function.

scholarly journals Oxygen-independent disulfide bond formation in VEGF-A and CA9

2021 ◽  
pp. 100505
Author(s):  
Fiana Levitin ◽  
Sandy Che-Eun Serena Lee ◽  
Stephanie Hulme ◽  
Ryan A. Rumantir ◽  
Amy S. Wong ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation
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