Sulfur-34S stable isotope labeling of amino acids for quantification (SULAQ34) of proteomic changes in Pseudomonas fluorescens during naphthalene degradation. Academic Article uri icon

Overview

abstract

  • The relative quantification of proteins is one of the major techniques used to elucidate physiological reactions. Because it allows one to avoid artifacts due to chemical labeling, the metabolic introduction of heavy isotopes into proteins and peptides is the preferred method for relative quantification. For eukaryotic cells, stable isotope labeling by amino acids in cell culture (SILAC) has become the gold standard and can be readily applied in a vast number of scenarios. In the microbial realm, with its highly versatile metabolic capabilities, SILAC is often not feasible, and the use of other (13)C or (15)N labeled substrates might not be practical. Here, the incorporation of heavy sulfur isotopes is shown to be a useful alternative. We introduce (34)S stable isotope labeling of amino acids for quantification and the corresponding tools required for spectra extraction and disintegration of the isotopic overlaps caused by the small mass shift. As proof of principle, we investigated the proteomic changes related to naphthalene degradation in P. fluorescens ATCC 17483 and uncovered a specific oxidative-stress-like response.

publication date

  • April 19, 2013

Research

keywords

  • Bacterial Proteins
  • Environmental Pollutants
  • Naphthalenes
  • Pseudomonas fluorescens

Identity

PubMed Central ID

  • PMC3734569

Scopus Document Identifier

  • 84881102933

Digital Object Identifier (DOI)

  • 10.1074/mcp.M112.025627

PubMed ID

  • 23603340

Additional Document Info

volume

  • 12

issue

  • 8