Proteomics of Arabidopsis redox proteins in response to methyl jasmonate

Sophie Alvarez, Mengmeng Zhu, Sixue Chen

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

Protein redox regulation is increasingly recognized as an important switch of protein activity in yeast, bacteria, mammals and plants. In this study, we identified proteins with potential thiol switches involved in jasmonate signaling, which is essential for plant defense. Methyl jasmonate (MeJA) treatment led to enhanced production of hydrogen peroxide in Arabidopsis leaves and roots, indicating in vivo oxidative stress. With monobromobimane (mBBr) labeling to capture oxidized sulfhydryl groups and 2D gel separation, a total of 35 protein spots that displayed significant redox and/or total protein expression changes were isolated. Using LC-MS/MS, the proteins in 33 spots were identified in both control and MeJA-treated samples. By comparative analysis of mBBr and SyproRuby gel images, we were able to determine many proteins that were redox responsive and proteins that displayed abundance changes in response to MeJA. Interestingly, stress and defense proteins constitute a large group that responded to MeJA. In addition, many cysteine residues involved in the disulfide dynamics were mapped based on tandem MS data. Identification of redox proteins and their cysteine residues involved in the redox regulation allows for a deeper understanding of the jasmonate signaling networks.

Original languageEnglish (US)
Pages (from-to)30-40
Number of pages11
JournalJournal of Proteomics
Volume73
Issue number1
DOIs
StatePublished - Nov 2 2009

Fingerprint

Arabidopsis Proteins
Proteomics
Oxidation-Reduction
Proteins
Cysteine
Gels
Switches
methyl jasmonate
Mammals
Oxidative stress
Heat-Shock Proteins
Arabidopsis
Sulfhydryl Compounds
Disulfides
Hydrogen Peroxide
Yeast
Labeling
Oxidative Stress
Yeasts
Bacteria

Keywords

  • 2-DE
  • Arabidopsis
  • Mass Spectrometry
  • Methyl jasmonate
  • Redox proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

Cite this

Proteomics of Arabidopsis redox proteins in response to methyl jasmonate. / Alvarez, Sophie; Zhu, Mengmeng; Chen, Sixue.

In: Journal of Proteomics, Vol. 73, No. 1, 02.11.2009, p. 30-40.

Research output: Contribution to journalArticle

Alvarez, Sophie ; Zhu, Mengmeng ; Chen, Sixue. / Proteomics of Arabidopsis redox proteins in response to methyl jasmonate. In: Journal of Proteomics. 2009 ; Vol. 73, No. 1. pp. 30-40.
@article{40e79b4e4ae34366bf3900666d915fdc,
title = "Proteomics of Arabidopsis redox proteins in response to methyl jasmonate",
abstract = "Protein redox regulation is increasingly recognized as an important switch of protein activity in yeast, bacteria, mammals and plants. In this study, we identified proteins with potential thiol switches involved in jasmonate signaling, which is essential for plant defense. Methyl jasmonate (MeJA) treatment led to enhanced production of hydrogen peroxide in Arabidopsis leaves and roots, indicating in vivo oxidative stress. With monobromobimane (mBBr) labeling to capture oxidized sulfhydryl groups and 2D gel separation, a total of 35 protein spots that displayed significant redox and/or total protein expression changes were isolated. Using LC-MS/MS, the proteins in 33 spots were identified in both control and MeJA-treated samples. By comparative analysis of mBBr and SyproRuby gel images, we were able to determine many proteins that were redox responsive and proteins that displayed abundance changes in response to MeJA. Interestingly, stress and defense proteins constitute a large group that responded to MeJA. In addition, many cysteine residues involved in the disulfide dynamics were mapped based on tandem MS data. Identification of redox proteins and their cysteine residues involved in the redox regulation allows for a deeper understanding of the jasmonate signaling networks.",
keywords = "2-DE, Arabidopsis, Mass Spectrometry, Methyl jasmonate, Redox proteins",
author = "Sophie Alvarez and Mengmeng Zhu and Sixue Chen",
year = "2009",
month = "11",
day = "2",
doi = "10.1016/j.jprot.2009.07.005",
language = "English (US)",
volume = "73",
pages = "30--40",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Proteomics of Arabidopsis redox proteins in response to methyl jasmonate

AU - Alvarez, Sophie

AU - Zhu, Mengmeng

AU - Chen, Sixue

PY - 2009/11/2

Y1 - 2009/11/2

N2 - Protein redox regulation is increasingly recognized as an important switch of protein activity in yeast, bacteria, mammals and plants. In this study, we identified proteins with potential thiol switches involved in jasmonate signaling, which is essential for plant defense. Methyl jasmonate (MeJA) treatment led to enhanced production of hydrogen peroxide in Arabidopsis leaves and roots, indicating in vivo oxidative stress. With monobromobimane (mBBr) labeling to capture oxidized sulfhydryl groups and 2D gel separation, a total of 35 protein spots that displayed significant redox and/or total protein expression changes were isolated. Using LC-MS/MS, the proteins in 33 spots were identified in both control and MeJA-treated samples. By comparative analysis of mBBr and SyproRuby gel images, we were able to determine many proteins that were redox responsive and proteins that displayed abundance changes in response to MeJA. Interestingly, stress and defense proteins constitute a large group that responded to MeJA. In addition, many cysteine residues involved in the disulfide dynamics were mapped based on tandem MS data. Identification of redox proteins and their cysteine residues involved in the redox regulation allows for a deeper understanding of the jasmonate signaling networks.

AB - Protein redox regulation is increasingly recognized as an important switch of protein activity in yeast, bacteria, mammals and plants. In this study, we identified proteins with potential thiol switches involved in jasmonate signaling, which is essential for plant defense. Methyl jasmonate (MeJA) treatment led to enhanced production of hydrogen peroxide in Arabidopsis leaves and roots, indicating in vivo oxidative stress. With monobromobimane (mBBr) labeling to capture oxidized sulfhydryl groups and 2D gel separation, a total of 35 protein spots that displayed significant redox and/or total protein expression changes were isolated. Using LC-MS/MS, the proteins in 33 spots were identified in both control and MeJA-treated samples. By comparative analysis of mBBr and SyproRuby gel images, we were able to determine many proteins that were redox responsive and proteins that displayed abundance changes in response to MeJA. Interestingly, stress and defense proteins constitute a large group that responded to MeJA. In addition, many cysteine residues involved in the disulfide dynamics were mapped based on tandem MS data. Identification of redox proteins and their cysteine residues involved in the redox regulation allows for a deeper understanding of the jasmonate signaling networks.

KW - 2-DE

KW - Arabidopsis

KW - Mass Spectrometry

KW - Methyl jasmonate

KW - Redox proteins

UR - http://www.scopus.com/inward/record.url?scp=70349983351&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=70349983351&partnerID=8YFLogxK

U2 - 10.1016/j.jprot.2009.07.005

DO - 10.1016/j.jprot.2009.07.005

M3 - Article

C2 - 19628057

AN - SCOPUS:70349983351

VL - 73

SP - 30

EP - 40

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

IS - 1

ER -