Redox properties of the A-domain of the HMGB1 protein

Debashish Sahu; Priyanka Debnath; Yuki Takayama; Junji Iwahara

doi:10.1016/j.febslet.2008.09.061

Redox properties of the A-domain of the HMGB1 protein

Debashish Sahu, Priyanka Debnath, Yuki Takayama, Junji Iwahara

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the real-time kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. Thermodynamic experiments showed that the Cys22-Cys44 disulfide bond stabilizes the folded state of the protein. These data suggest that the oxidized HMGB1 may accumulate even in cells under oxidative stress. Structured summary: MINT-6795963:txn (uniprotkb:P10599) and HMGB1 (uniprotkb:P09429) bind (MI:0408) by nuclear magnetic resonance (MI:0077).

Original language	English (US)
Pages (from-to)	3973-3978
Number of pages	6
Journal	FEBS Letters
Volume	582
Issue number	29
DOIs	https://doi.org/10.1016/j.febslet.2008.09.061
State	Published - Dec 10 2008

Keywords

Disulfide bond
HMGB1
Kinetics
NMR spectroscopy
Redox
Thermodynamics

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2008.09.061

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title = "Redox properties of the A-domain of the HMGB1 protein",

abstract = "The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the real-time kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. Thermodynamic experiments showed that the Cys22-Cys44 disulfide bond stabilizes the folded state of the protein. These data suggest that the oxidized HMGB1 may accumulate even in cells under oxidative stress. Structured summary: MINT-6795963:txn (uniprotkb:P10599) and HMGB1 (uniprotkb:P09429) bind (MI:0408) by nuclear magnetic resonance (MI:0077).",

keywords = "Disulfide bond, HMGB1, Kinetics, NMR spectroscopy, Redox, Thermodynamics",

author = "Debashish Sahu and Priyanka Debnath and Yuki Takayama and Junji Iwahara",

note = "Funding Information: We thank Dr. Marius Clore for supporting preliminary studies; Drs. Wayne Bolen and Luis Marcelo Holthauzen for assisting in CD analysis; and Dr. David Konkel for critically reading the manuscript. This publication was made possible by Grant ES006676 from the National Institute of Environmental Health Sciences.",

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doi = "10.1016/j.febslet.2008.09.061",

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AU - Sahu, Debashish

AU - Debnath, Priyanka

AU - Takayama, Yuki

AU - Iwahara, Junji

N1 - Funding Information: We thank Dr. Marius Clore for supporting preliminary studies; Drs. Wayne Bolen and Luis Marcelo Holthauzen for assisting in CD analysis; and Dr. David Konkel for critically reading the manuscript. This publication was made possible by Grant ES006676 from the National Institute of Environmental Health Sciences.

PY - 2008/12/10

Y1 - 2008/12/10

N2 - The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the real-time kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. Thermodynamic experiments showed that the Cys22-Cys44 disulfide bond stabilizes the folded state of the protein. These data suggest that the oxidized HMGB1 may accumulate even in cells under oxidative stress. Structured summary: MINT-6795963:txn (uniprotkb:P10599) and HMGB1 (uniprotkb:P09429) bind (MI:0408) by nuclear magnetic resonance (MI:0077).

AB - The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the real-time kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. Thermodynamic experiments showed that the Cys22-Cys44 disulfide bond stabilizes the folded state of the protein. These data suggest that the oxidized HMGB1 may accumulate even in cells under oxidative stress. Structured summary: MINT-6795963:txn (uniprotkb:P10599) and HMGB1 (uniprotkb:P09429) bind (MI:0408) by nuclear magnetic resonance (MI:0077).

KW - Disulfide bond

KW - HMGB1

KW - Kinetics

KW - NMR spectroscopy

KW - Redox

KW - Thermodynamics

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Redox properties of the A-domain of the HMGB1 protein

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