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Thiol‐based redox proteins in abscisic acid and methyl jasmonate signaling in B rassica napus guard cells
Author(s) -
Zhu Mengmeng,
Zhu Ning,
Song Wenyuan,
Harmon Alice C.,
Assmann Sarah M.,
Chen Sixue
Publication year - 2014
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12490
Subject(s) - guard cell , abscisic acid , methyl jasmonate , biochemistry , redox , cysteine , chemistry , microbiology and biotechnology , biology , enzyme , gene , organic chemistry
Summary Reversibly oxidized cysteine sulfhydryl groups serve as redox sensors or targets of redox sensing that are important in various physiological processes. However, little is known about redox‐sensitive proteins in guard cells and how they function in stomatal signaling. In this study, B rassica napus guard‐cell proteins altered by redox in response to abscisic acid ( ABA ) or methyl jasmonate ( M e JA ) were identified by complementary proteomics approaches, saturation differential in‐gel electrophoresis and isotope‐coded affinity tagging. In total, 65 and 118 potential redox‐responsive proteins were identified in ABA ‐ and M e JA ‐treated guard cells, respectively. All the proteins contain at least one cysteine, and over half of them are predicted to form intra‐molecular disulfide bonds. Most of the proteins fall into the functional groups of ‘energy’, ‘stress and defense’ and ‘metabolism’. Based on the peptide sequences identified by mass spectrometry, 30 proteins were common to ABA ‐ and M e JA ‐treated samples. A total of 44 cysteines were mapped in the identified proteins, and their levels of redox sensitivity were quantified. Two of the proteins, a sucrose non‐fermenting 1‐related protein kinase and an isopropylmalate dehydrogenase, were confirmed to be redox‐regulated and involved in stomatal movement. This study creates an inventory of potential redox switches, and highlights a protein redox regulatory mechanism in ABA and M e JA signal transduction in guard cells.