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CBC/RBC seminar - Dr. Eranthie Weerapana, Boston College

Chemical-proteomic Strategies to Investigate Reactive Cysteines

4:00 pm – 5:00 pm
via Zoom presentation
Meeting ID: 981 6169 6610 Passcode: 444813
Diana Bonham, (402) 472-2932,
Cysteine residues are critical to the catalytic and regulatory functions of diverse proteins including proteases, oxidoreductases and kinases. Although the majority of catalytic cysteine residues are well annotated, the identity and endogenous functions of regulatory and metal-binding cysteines are poorly understood. Regulatory cysteines are often located distal to the catalytic or ligand-binding sites of proteins and regulate protein function through posttranslational modifications, such as oxidation. Metal-binding cysteines provide coordination to a variety of metal ions, including zinc and iron, and are essential to maintaining the structure and function of diverse metalloproteins. Oxidation and coordination to metal ions result in distinct changes in cysteine reactivity, and we have developed a suite of chemoproteomic approaches for monitoring these cysteine-reactivity changes directly in cell lysates and living cells. Our efforts have generated a suite of chemical probes to investigate cysteine function, and unearthed previously uncharacterized functional cysteines implicated in catalysis and regulation.

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This event originated in Biochemistry.