Proteome-wide Quantification and Characterization of Oxidation-Sensitive Cysteines in Pathogenic Bacteria

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• 作者：Xin Deng¹ ; Eranthie Weerapana² ; ⁵ ; ⁶ ; Olesya Ulanovskaya⁵ ; ⁶ ; Fei Sun¹ ; Haihua Liang¹ ; Quanjiang Ji¹ ; Yan Ye³ ; Ye Fu¹ ; Lu Zhou¹ ; Jiaxin Li³ ; Haiyan Zhang¹ ; Chu Wang⁵ ; ⁶ ; Sophie Alvarez⁴ ; Leslie M. Hicks⁴ ; Lefu Lan⁷ ; Min Wu³ ; Benjamin F. Cravatt⁵ ; ⁶ ; ^{cravatt@scripps.edu} ; Chuan He¹ ; ^{chuanhe@uchicago.edu}
• 刊名：Cell Host Microbe
• 出版年：2013
• 出版时间：13 March, 2013
• 年：2013
• 卷：13
• 期：3
• 页码：358-370
• 全文大小：1322 K

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Summary

Thiol-group oxidation of active and allosteric cysteines is a widespread regulatory posttranslational protein modification. Pathogenic bacteria, including Pseudomonas aeruginosa and Staphylococcus aureus, use regulatory cysteine oxidation to respond to and overcome reactive oxygen species (ROS) encountered in the host environment. To obtain a proteome-wide view of oxidation-sensitive cysteines in these two pathogens, we employed a competitive activity-based protein profiling approach to globally quantify hydrogen peroxide (H₂O₂) reactivity with cysteines across bacterial proteomes. We identified ¡«200 proteins containing H₂O₂-sensitive cysteines, including metabolic enzymes, transcription factors, and uncharacterized proteins. Additional biochemical and genetic studies identified an oxidation-responsive cysteine in the master quorum-sensing regulator LasR and redox-regulated activities for acetaldehyde dehydrogenase ExaC, arginine deiminase ArcA, and glyceraldehyde 3-phosphate dehydrogenase. Taken together, our data indicate that pathogenic bacteria exhibit a complex, multilayered response to ROS that includes the rapid adaption of metabolic pathways to oxidative-stress challenge.