Proteomics studies of post-translational modifications in plants

Jae Kwon Sun, Young Choi Eun, Jung Choi Yoon, Ji Hoon Ahn, Ohkmae Kim

Research output: Contribution to journalArticle

58 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 1

Fingerprint

post-translational modification
Post Translational Protein Processing
Proteomics
proteomics
Glycosylphosphatidylinositols
Proteins
proteins
Ubiquitination
Affinity Chromatography
Immunoprecipitation
Mass Spectrometry
instrumentation
affinity chromatography
Metals
Phosphorylation
phosphorylation
methodology
metals
mass spectrometry
sampling

Keywords

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

ASJC Scopus subject areas

  • Plant Science

Cite this

Proteomics studies of post-translational modifications in plants. / Sun, Jae Kwon; Eun, Young Choi; Yoon, Jung Choi; Ahn, Ji Hoon; Kim, Ohkmae.

In: Journal of Experimental Botany, Vol. 57, No. 7, 01.04.2006, p. 1547-1551.

Research output: Contribution to journalArticle

Sun, Jae Kwon ; Eun, Young Choi ; Yoon, Jung Choi ; Ahn, Ji Hoon ; Kim, Ohkmae. / Proteomics studies of post-translational modifications in plants. In: Journal of Experimental Botany. 2006 ; Vol. 57, No. 7. pp. 1547-1551.
@article{e55e3ecfdd35477199af48b0806c056a,
title = "Proteomics studies of post-translational modifications in plants",
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",
author = "Sun, {Jae Kwon} and Eun, {Young Choi} and Yoon, {Jung Choi} and Ahn, {Ji Hoon} and Ohkmae Kim",
year = "2006",
month = "4",
day = "1",
doi = "10.1093/jxb/erj137",
language = "English",
volume = "57",
pages = "1547--1551",
journal = "Journal of Experimental Botany",
issn = "0022-0957",
publisher = "Oxford University Press",
number = "7",

}

TY - JOUR

T1 - Proteomics studies of post-translational modifications in plants

AU - Sun, Jae Kwon

AU - Eun, Young Choi

AU - Yoon, Jung Choi

AU - Ahn, Ji Hoon

AU - Kim, Ohkmae

PY - 2006/4/1

Y1 - 2006/4/1

N2 - 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.

AB - 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.

KW - Glycosylphosphatidylinositol

KW - Phosphorylation

KW - Plant

KW - Post-translational modification

KW - Proteomics

KW - Ubiquitination

UR - http://www.scopus.com/inward/record.url?scp=33646248895&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33646248895&partnerID=8YFLogxK

U2 - 10.1093/jxb/erj137

DO - 10.1093/jxb/erj137

M3 - Article

C2 - 16551683

AN - SCOPUS:33646248895

VL - 57

SP - 1547

EP - 1551

JO - Journal of Experimental Botany

JF - Journal of Experimental Botany

SN - 0022-0957

IS - 7

ER -