Proteomics studies of post-translational modifications in plants

Jae Kwon Sun, Young Choi Eun, Jung Choi Yoon, Hoon Ahn Ji, Ohkmae K. Park

Research output: Contribution to journalReview article

59 Citations (Scopus)

Abstract

Post-translational modifications of proteins greatly increase protein complexity and dynamics, co-ordinating the intricate regulation of biological events. The global identification of post-translational modifications is a difficult task that is currently accelerated by advances in proteomics techniques. There has been significant development in sample preparation methods and mass spectrometry instrumentation. To reduce the complexity and to increase the amount of modified proteins available for analysis, proteins are usually subjected to prefractionation such as chromatographic purification and affinity enrichment. In this review, the post-translational modification studies in plants are summarized. The sample preparation strategies applied to each study are also described. These include affinity-based enrichment methods, immobilized metal affinity chromatography and immunoprecipitation used for phosphorylation and ubiquitination studies, respectively, and the phase partitioning approach for glycosylphosphatidylinositol modification studies.

Original languageEnglish
Pages (from-to)1547-1551
Number of pages5
JournalJournal of experimental botany
Volume57
Issue number7
DOIs
Publication statusPublished - 2006 Apr

Keywords

  • Glycosylphosphatidylinositol
  • Phosphorylation
  • Plant
  • Post-translational modification
  • Proteomics
  • Ubiquitination

ASJC Scopus subject areas

  • Physiology
  • Plant Science

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