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JXB Advance Access originally published online on March 21, 2006
Journal of Experimental Botany 2006 57(7):1547-1551; doi:10.1093/jxb/erj137
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© The Author [2006]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

Proteomics studies of post-translational modifications in plants

Sun Jae Kwon1, Eun Young Choi1, Yoon Jung Choi2, Ji Hoon Ahn1 and Ohkmae K Park1,*

1School of Life Sciences and Biotechnology, Korea University, Anam-dong, Seongbuk-gu, Seoul 136-701, Korea
2Department of Life Sciences, Gwangju Institute of Science and Technology (GIST), Gwangju 500-712, Korea

*To whom correspondence should be addressed. E-mail: omkim{at}korea.ac.kr

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.

Key words: Glycosylphosphatidylinositol, phosphorylation, plant, post-translational modification, proteomics, ubiquitination


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