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Target-selective protein S-nitrosylation by sequence motif recognition.

Jie Jia1, Abul Arif1, Fulvia Terenzi1

  • 1Department of Cellular and Molecular Medicine, The Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.

Cell
|November 24, 2014
PubMed
Summary

Researchers discovered a new protein complex that modifies proteins using nitric oxide (NO). This complex, involving inducible nitric oxide synthase (iNOS), S100A8, and S100A9, precisely targets specific protein sites, similar to phosphorylation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • S-nitrosylation is a key nitric oxide (NO)-mediated posttranslational modification regulating cell function.
  • While numerous S-nitrosylated proteins are known, the enzymes (S-nitrosylases) and mechanisms for site-selective modification remain largely uncharacterized.

Purpose of the Study:

  • To identify and characterize novel S-nitrosylase complexes.
  • To elucidate the mechanisms underlying site-selective S-nitrosylation.
  • To identify sequence motifs recognized by S-nitrosylases.

Main Methods:

  • Proteomic analysis to identify S-nitrosylated proteins.
  • Biochemical assays to characterize enzyme activity and complex formation.
  • Site-directed mutagenesis to determine the role of specific sequence motifs.

Main Results:

  • A novel heterotrimeric complex of inducible nitric oxide synthase (iNOS), S100A8, and S100A9 was identified as a stimulus-inducible S-nitrosylase.
  • S100A9 acts as a transnitrosylase, transferring NO from iNOS to target proteins.
  • S100A8 and S100A9 collaborate to direct site selection, recognizing a conserved I/L-X-C-X2-D/E motif.
  • Proteomic analysis identified novel protein targets of this iNOS-S100A8/A9 complex.

Conclusions:

  • The iNOS-S100A8/A9 complex represents a primary mechanism for stimulus-dependent S-nitrosylation.
  • Site-selective S-nitrosylation, mediated by specific sequence motifs, parallels mechanisms of protein phosphorylation.
  • This discovery provides new insights into NO signaling pathways and protein regulation.