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JXB Advance Access published online on March 21, 2006
Journal of Experimental Botany, 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
Received August 31, 2005
Accepted January 25, 2006

Plant Proteomics Special Issue Article

Proteomics studies of post-translational modifications in plants

Sun Jae Kwon 1, Eun Young Choi 1, Yoon Jung Choi 2, Ji Hoon Ahn 1, and Ohkmae K. Park 1 *

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

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


  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.

Keywords: Glycosylphosphatidylinositol; phosphorylation; plant; post-translational modification; proteomics; ubiquitination.
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