Abstract
During oxidative stress in Escherichiacoli, the SufABCDSE stress response pathway mediates iron-sulfur (Fe-S) cluster biogenesis rather than the Isc pathway. To determine why the Suf pathway is favored under stress conditions, the stress response SufS-SufE sulfur transfer pathway and the basal housekeeping IscS-IscU pathway were directly compared. We found that SufS-SufE cysteine desulfurase activity is significantly higher than IscS-IscU at physiological cysteine concentrations and after exposure to H(2)O(2). Mass spectrometry analysis demonstrated that IscS-IscU is more susceptible than SufS-SufE to oxidative modification by H(2)O(2). These important results provide biochemical insight into the stress resistance of the Suf pathway.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Biocatalysis / drug effects
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Carbon-Sulfur Lyases / genetics
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Carbon-Sulfur Lyases / metabolism*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cysteine / metabolism
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Hydrogen Peroxide / pharmacology
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Iron-Sulfur Proteins / genetics
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Iron-Sulfur Proteins / metabolism*
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Kinetics
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Lyases / genetics
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Lyases / metabolism*
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Mass Spectrometry
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Oxidants / pharmacology
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Oxidation-Reduction
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Oxidative Stress*
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Substrate Specificity
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Sulfur / metabolism*
Substances
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Carrier Proteins
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Escherichia coli Proteins
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Iron-Sulfur Proteins
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IscU protein, E coli
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Oxidants
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Suf E protein, E coli
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Sulfur
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Hydrogen Peroxide
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Lyases
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Carbon-Sulfur Lyases
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cysteine desulfurase
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selenocysteine lyase
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Cysteine