A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Seth, D; Hess, DT; Hausladen, A; Wang, L; Wang, Y-J; Stamler, JS

Published Date

  • February 1, 2018

Published In

Volume / Issue

  • 69 / 3

Start / End Page

  • 451 - 464.e6

PubMed ID

  • 29358078

Pubmed Central ID

  • 29358078

Electronic International Standard Serial Number (EISSN)

  • 1097-4164

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2017.12.025

Language

  • eng

Conference Location

  • United States