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 techni...

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Published inJournal of experimental botany Vol. 57; no. 7; pp. 1547 - 1551
Main Authors Kwon, Sun Jae, Choi, Eun Young, Choi, Yoon Jung, Ahn, Ji Hoon, Park, Ohkmae K
Format Journal Article Conference Proceeding
LanguageEnglish
Published Oxford Oxford University Press 01.04.2006
Oxford Publishing Limited (England)
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ObjectType-Review-1
ISSN:0022-0957
1460-2431
DOI:10.1093/jxb/erj137