3 years ago

A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation

A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation
S-nitrosylation, the oxidative modification of Cys residues by nitric oxide (NO) to form S-nitrosothiols (SNOs), modifies all main classes of proteins and provides a fundamental redox-based cellular signaling mechanism. However, in contrast to other post-translational protein modifications, S-nitrosylation is generally considered to be non-enzymatic, involving multiple chemical routes. We report here that endogenous protein S-nitrosylation in the model organism E. coli depends principally upon the enzymatic activity of the hybrid cluster protein Hcp, employing NO produced by nitrate reductase. Anaerobiosis on nitrate induces both Hcp and nitrate reductase, thereby resulting in the S-nitrosylation-dependent assembly of a large interactome including enzymes that generate NO (NO synthase), synthesize SNO-proteins (SNO synthase), and propagate SNO-based signaling (trans-nitrosylases) to regulate cell motility and metabolism. Thus, protein S-nitrosylation by NO in E. coli is essentially enzymatic, and the potential generality of the multiplex enzymatic mechanism that we describe may support a re-conceptualization of NO-based cellular signaling.

Graphical abstract

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Teaser

Protein S-nitrosylation by nitric oxide is generally thought to be non-enzymatic. Seth et al. demonstrate that endogenous S-nitrosylation in E. coli depends upon enzymatic activity of the hybrid cluster protein Hcp and involves assembly of an Hcp interactome including enzymes that generate NO, synthesize SNO-proteins, and propagate SNO-based signaling.

Publisher URL: www.sciencedirect.com/science

DOI: S1097276517309826

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