Identification of Mammalian Protein Complexes by Lentiviral-Based Affinity Purification and Mass Spectrometry

Zuyao Ni, Jonathan B. Olsen, Andrew Emili, Jack F. Greenblatt

Research output: Chapter in Book/Report/Conference proceedingChapter

11 Scopus citations

Abstract

Protein complexes and protein–protein interactions (PPIs) are fundamental for most biological functions. Deciphering the extensive protein interaction networks that occur within cellular contexts has become a logical extension to the human genome project. Proteome-scale interactome analysis of mammalian systems requires efficient methods for accurately detecting PPIs with specific considerations for the intrinsic technical challenges of mammalian genome manipulation. In this chapter, we outline in detail an innovative lentiviral-based functional proteomic approach that can be used to rapidly characterize protein complexes from a broad range of mammalian cell lines. This method integrates the following key features: (1) lentiviral elements for efficient delivery of tagged constructs into mammalian cell lines; (2) site-specific Gateway™ recombination sites for easy cloning; (3) versatile epitope-tagging system for flexible affinity purification strategies; and (4) LC-MS-based protein identification using tandem mass spectrometry.

Original languageEnglish (US)
Title of host publicationNetwork Biology
Subtitle of host publicationMethods and Applications
PublisherHumana Press Inc.
Pages31-45
Number of pages15
ISBN (Print)9781617792755
DOIs
StatePublished - 2011
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume781
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • Affinity purification
  • Gateway™ cloning
  • Lentivirus
  • Mass spectrometry
  • Protein complexes
  • Protein–protein interactions

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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