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A GTP affinity probe for proteomics highlights flexibility in purine nucleotide selectivity

Academic Article
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Overview

authors

  • Cisar, E. A. G.
  • Nguyen, N.
  • Rosen, Hugh

publication date

  • March 2013

journal

  • Journal of the American Chemical Society  Journal

abstract

  • GTP affinity probes are important tools for the study of GTP-binding proteins, and proteomic profiling is a powerful methodology well suited for the study of such a diverse class of proteins. Here, we synthesize and characterize a photoreactive GTP affinity probe that covalently photocross-links to protein targets and has an alkyne handle for click chemistry conjugation to reporter tags. The GTP-BP-yne probe facilitated identification of a variety of GTP-binding proteins by mass spectrometry, such as small GTPases and members of the GTP1/OBG family. Several ATP-binding proteins were also identified, highlighting variability in purine nucleotide selectivity of some proteins, and the probe was used to elucidate targets' relative nucleotide selectivities. The GTP-BP-yne probe will be a useful tool for the study of GTP-binding proteins, especially when targets of interest are not known a priori.

subject areas

  • Adenosine Triphosphate
  • Affinity Labels
  • GTP-Binding Proteins
  • Guanosine Triphosphate
  • HEK293 Cells
  • Humans
  • Protein Binding
  • Proteomics
  • Purine Nucleotides
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja400839e

PubMed ID

  • 23473570
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Additional Document Info

start page

  • 4676

end page

  • 4679

volume

  • 135

issue

  • 12

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