Lecture will be held in English

Hosted by

Štěpánka Vaňáčová

About the lecture

Lysine-cysteine Redox Switches in Proteins

Modifications of cysteine residues in redox-sensitive proteins are key to redox signaling and stress response in all organisms with disulfide bridges between two proximal cysteines being a prevalent form. We recently discovered a novel type of redox switch that comprises lysine and cysteine residues covalently linked by a nitrogen–oxygen–sulfur (NOS) bridge. Our systematic survey of the whole protein structure database disclosed that NOS bridges are ubiquitous redox switches in proteins of all domains of life and are found in numerous structural motifs and chemical variants. In several instances, lysines are observed in simultaneous covalent linkage with two cysteines, forming a sulfur–oxygen–nitrogen–oxygen–sulfur (SONOS) bridge with a trivalent nitrogen, which constitutes an unusual native branching cross-link. In many proteins, the NOS switch contains a functionally essential lysine with direct roles in enzyme catalysis or binding of substrates, DNA or effectors, linking lysine chemistry and redox biology as a novel regulatory principle. NOS/SONOS switches are frequently found in proteins from human and plant pathogens, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and also in many human proteins with established roles in gene expression, redox signaling and homeostasis in physiological and pathophysiological conditions. I will discuss the chemical and biological implications of the novel redox switches.

Registration for lunch with the speaker /for Ph.D. students/

The sponsored lunch usually takes place in the Campus River restaurant. Please meet the speaker and other students at 12:45 at the reception desk at the main entrance (building B22, see the map below).