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Related Concept Videos

DNA Microarrays02:34

DNA Microarrays

Microarrays are high-throughput and relatively inexpensive assays that can be automated to analyze large quantities of data at a time. They are used in genome-wide studies to compare gene or protein expression under two varied conditions, such as healthy and diseased states. Microarrays consist of glass or silica slides on which probe molecules are covalently attached through surface functionalization. Most commonly, the slides are prepared through the chemisorption of silanes to silica...

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Nitropeptide Profiling and Identification Illustrated by Angiotensin II
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A protein microarray-based analysis of S-nitrosylation.

Matthew W Foster1, Michael T Forrester, Jonathan S Stamler

  • 1Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 30, 2009
PubMed
Summary
This summary is machine-generated.

Nitric oxide (NO) influences cells via protein S-nitrosylation. This study reveals multifactorial determinants of S-nitrosylation specificity, including protein structure and NO donor design, crucial for understanding cellular signaling.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Nitric oxide (NO) is a key cellular signaling molecule.
  • Protein S-nitrosylation, a modification by NO, regulates numerous biological processes.
  • The specificity of S-nitrosylation, despite NO's promiscuity, is not fully understood.

Purpose of the Study:

  • To investigate the determinants of protein S-nitrosylation specificity.
  • To identify target proteins and factors influencing S-nitrosylation by S-nitrosothiols (SNOs).
  • To explore rational design strategies for SNOs to achieve target specificity.

Main Methods:

  • Development of a protein microarray-based approach for high-throughput screening.
  • Analysis of S-nitrosylation patterns in yeast and human proteomes.
  • Investigation of the influence of protein structure, Cys thiol location, and NO donor properties.

Main Results:

  • Identification of extensive sets of S-nitrosylation targets in yeast and human cells.
  • Observed enrichment of S-nitrosylation at active-site Cys residues within alpha-helices and catalytic loops.
  • Demonstrated that protein secondary structure and thiol nucleophilicity alone do not fully explain specificity.
  • Revealed significant impact of NO donor stereochemistry, structure, and allosteric effectors on S-nitrosylation efficiency.

Conclusions:

  • Protein S-nitrosylation specificity is multifactorial, involving target protein properties and S-nitrosylating species.
  • High-throughput proteomic analysis reveals determinants often missed by other methods.
  • Rational design of S-nitrosothiols can achieve specific protein modification, offering therapeutic potential.