TY - JOUR
T1 - Nitration is exclusive to defense-related PR-1, PR-3 and PR-5 proteins in tobacco leaves
AU - Takahashi, Misa
AU - Shigeto, Jun
AU - Izumi, Shunsuke
AU - Yoshizato, Katsutoshi
AU - Morikawa, Hiromichi
N1 - Publisher Copyright:
© 2016 Taylor & Francis Group, LLC.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2016/7/2
Y1 - 2016/7/2
N2 - 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.
AB - 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.
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U2 - 10.1080/15592324.2016.1197464
DO - 10.1080/15592324.2016.1197464
M3 - Article
C2 - 27301959
AN - SCOPUS:84982952519
SN - 1559-2316
VL - 11
JO - Plant Signaling and Behavior
JF - Plant Signaling and Behavior
IS - 7
M1 - e1197464
ER -