Nitration is exclusive to defense-related PR-1, PR-3 and PR-5 proteins in tobacco leaves

被引:11
|
作者
Takahashi, Misa [1 ]
Shigeto, Jun [1 ]
Izumi, Shunsuke [1 ]
Yoshizato, Katsutoshi [2 ]
Morikawa, Hiromichi [1 ]
机构
[1] Hiroshima Univ, Dept Math & Life Sci, Higashihiroshima, Japan
[2] Hiroshima Univ, Dept Biol Sci, Higashihiroshima, Hiroshima, Japan
基金
日本学术振兴会;
关键词
Apoplast; defense/immunity-related proteins; nitrogen dioxide; pathogenesis-related proteins; PR-1; PR-3; PR-5; protein tyrosine nitration; tobacco; vacuole; PATHOGENESIS-RELATED PROTEINS; ATMOSPHERIC NITROGEN-DIOXIDE; TYROSINE NITRATION; NITRIC-OXIDE; ARABIDOPSIS; REDUCTASE; INHIBITION; INDUCTION; TIME;
D O I
10.1080/15592324.2016.1197464
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein tyrosine nitration is an important post-translational modification. A variety of nitrated proteins are reported in Arabidopsis leaves and seedlings, sunflower hypocotyls, and pea roots. The identities of nitrated proteins are species-/organ-specific, and chloroplast proteins are most nitratable in leaves. However, precise mechanism is unclear. Here, we investigated nitroproteome in tobacco leaves following exposure to nitrogen dioxide. Proteins were extracted, electrophoresed and immunoblotted using an anti-3-nitrotyrosine antibody. Mass spectrometry and FASTA search identified for the first time an exclusive nitration of pathogenesis-related proteins, PR-1, PR-3 and PR-5, which are reportedly located in the apoplast or the vacuole. Furthermore, Tyr36 of thaumatin-like protein E2 was identfied as a nitration site. The underlying mechanism and physiological relevance are discussed.
引用
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页数:5
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