FEBS Letters
Volume 582, Issue 29 , Pages 3973-3978, 10 December 2008

Redox properties of the A-domain of the HMGB1 protein

Edited by Hans Eklund

Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, 301 University Blvd., 6.614D Basic Science Building, Galveston, TX 77555-0647, USA

Received 25 June 2008; received in revised form 27 August 2008; accepted 26 September 2008. published online 07 November 2008.

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)

Abbreviations: NMR, nuclear magnetic resonance, HSQC, heteronuclear single quantum coherence, DTT, dithiothreitol, GSH, reduced glutathione, GSSG, oxidized glutathione, Trx, thioredoxin, NADPH, reduced nicotinamide adenine dinucleotide phosphate, CD, circular dichroism

Keywords: HMGB1, Redox, Disulfide bond, Thermodynamics, Kinetics, NMR spectroscopy

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PII: S0014-5793(08)00877-6

doi:10.1016/j.febslet.2008.09.061

FEBS Letters
Volume 582, Issue 29 , Pages 3973-3978, 10 December 2008

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