Characterization of the Saccharomyces cerevisiae ATP-Interactome using the iTRAQ-SPROX Technique

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• 作者：M. Ariel Geer ; Michael C. Fitzgerald
• 关键词：Mass spectrometry ; Proteomics ; Thermodynamics ; Protein folding ; Chemical denaturation ; Ligand binding
• 刊名：Journal of The American Society for Mass Spectrometry
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：27
• 期：2
• 页码：233-243
• 全文大小：840 KB
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• 作者单位：M. Ariel Geer (1)
  Michael C. Fitzgerald (1)
  
  1. Department of Chemistry, Duke University, Durham, NC, 27708-0346, USA
  
• 刊物主题：Analytical Chemistry; Biotechnology; Organic Chemistry; Proteomics; Bioinformatics;
• 出版者：Springer US
• ISSN：1879-1123

文摘

The stability of proteins from rates of oxidation (SPROX) technique was used in combination with an isobaric mass tagging strategy to identify adenosine triphosphate (ATP) interacting proteins in the Saccharomyces cerevisiae proteome. The SPROX methodology utilized in this work enabled 373 proteins in a yeast cell lysate to be assayed for ATP interactions (both direct and indirect) using the non-hydrolyzable ATP analog, adenylyl imidodiphosphate (AMP-PNP). A total of 28 proteins were identified with AMP-PNP-induced thermodynamic stability changes. These protein hits included 14 proteins that were previously annotated as ATP-binding proteins in the Saccharomyces Genome Database (SGD). The 14 non-annotated ATP-binding proteins included nine proteins that were previously found to be ATP-sensitive in an earlier SPROX study using a stable isotope labeling with amino acids in cell culture (SILAC)-based approach. A bioinformatics analysis of the protein hits identified here and in the earlier SILAC-SPROX experiments revealed that many of the previously annotated ATP-binding protein hits were kinases, ligases, and chaperones. In contrast, many of the newly discovered ATP-sensitive proteins were not from these protein classes, but rather were hydrolases, oxidoreductases, and nucleic acid-binding proteins.