Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum

Irina Majoul; David Ferrari; Hans Dieter Söling

doi:10.1016/S0014-5793(96)01447-0

Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum

Irina Majoul, David Ferrari, Hans Dieter Söling^*

^*Corresponding author for this work

Institute of Biology

Georg August University Göttingen

70 Citations (Scopus)

Abstract

Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777-789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX-A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.

Original language	English
Journal	FEBS Letters
Volume	401
Issue number	2-3
Pages (from-to)	104-108
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(96)01447-0
Publication status	Published - 20.01.1997

Funding

This work was supported by grants from the Deutsche Forschungsgemeinschaft (project A3; SFB 236) and the Fonds der Chemischen Industrie given to H.D.S.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/S0014-5793(96)01447-0

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@article{b54dad33db504d3e89f7e642cddaeaee,

title = "Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum",

abstract = "Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777-789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX-A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.",

author = "Irina Majoul and David Ferrari and S{\"o}ling, \{Hans Dieter\}",

note = "Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft (project A3; SFB 236) and the Fonds der Chemischen Industrie given to H.D.S. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

year = "1997",

month = jan,

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doi = "10.1016/S0014-5793(96)01447-0",

language = "English",

volume = "401",

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T1 - Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum

AU - Majoul, Irina

AU - Ferrari, David

AU - Söling, Hans Dieter

N1 - Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft (project A3; SFB 236) and the Fonds der Chemischen Industrie given to H.D.S. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

PY - 1997/1/20

Y1 - 1997/1/20

N2 - Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777-789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX-A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.

AB - Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777-789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX-A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.

UR - https://www.scopus.com/pages/publications/0031031853

U2 - 10.1016/S0014-5793(96)01447-0

DO - 10.1016/S0014-5793(96)01447-0

M3 - Journal articles

C2 - 9013867

AN - SCOPUS:0031031853

SN - 0014-5793

VL - 401

SP - 104

EP - 108

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum

Abstract

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Research Areas and Centers

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