Proteomics studies of post-translational modifications in plants.
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.
School of Life Sciences and Biotechnology, Korea University, Anam-dong, Seongbuk-gu, Seoul 136-701, Korea.
Sun Jae
SJ
Kwon
Eun Young
EY
Choi
Yoon Jung
YJ
Choi
Ji Hoon
JH
Ahn
Ohkmae K
OK
Park
D002846:Chromatography, Affinity; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D047468:Immunoprecipitation; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D025801:Ubiquitin / Q000378:metabolism
D017261:Glycosylphosphatidylinositols; D010940:Plant Proteins; D025801:Ubiquitin