Isolation and characterization of plant protein complexes by mass spectrometry

Proteomics. 2011 May;11(9):1824-33. doi: 10.1002/pmic.201000635. Epub 2011 Apr 7.

Abstract

The components that enable cells and organisms to fulfill a plethora of chemical and physical reactions, including their ability to metabolize, replicate, repair and communicate with their environment are mostly based on the functioning of highly complex cellular machines which are to a large extent composed of proteins. With the development of MS techniques compatible with the analysis of minute amounts of biological material, it has become more and more feasible to dissect the composition and modification of these protein machineries. Indeed, new purification methods of protein complexes followed by MS analysis together with the genomic sequencing of various organisms - and in particular of crop species - now provide unforeseen insight to understand biological processes at a molecular level. We here review the current state of the art of in vivo protein complex isolation and their MS-based analytical characterization, emphasizing on the tandem affinity purification approach.

Publication types

  • Review

MeSH terms

  • Mass Spectrometry / methods*
  • Plant Proteins / analysis*
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism
  • Plants / metabolism
  • Proteome / analysis*
  • Proteome / isolation & purification
  • Proteome / metabolism
  • Proteomics / methods*
  • Proteomics / trends

Substances

  • Plant Proteins
  • Proteome