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Comparative analysis of salt‐responsive phosphoproteins in maize leaves using T i 4+ ‐ IMAC enrichment and ESI ‐ Q ‐ TOF MS
Author(s) -
Hu Yufeng,
Guo Shuangxi,
Li Xuexian,
Ren Xueqin
Publication year - 2013
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201200381
Subject(s) - phosphorylation , phosphopeptide , protein phosphorylation , chemistry , biochemistry , proteomics , peptide , isobaric labeling , halophyte , microbiology and biotechnology , biology , salinity , gene , protein kinase a , quantitative proteomics , ecology
Salinity is one of the most common abiotic stresses encountered by plants. Reversible protein phosphorylation is involved in plant defense processes against salinity stress. Here, we performed global phosphopeptide mapping through enrichment by our synthesized PVA ‐phosphate‐ T i 4+ IMAC coupled with subsequent identification by ESI ‐ Q ‐TOF MS . A total of 104 peptide sequences containing 139 phosphorylation sites were determined from 70 phosphoproteins of the control leaves. In contrast, 124 phosphopeptides containing 143 phosphorylated sites from 92 phosphoproteins were identified in salt‐stressed maize leaves. Compared with the control, 47 proteins were phosphorylated, 25 were dephosphorylated, and 45 overlapped. Among the 72 differential phosphoproteins, 35 were known salt stress response proteins and the rest had not been reported in the literature. To dissect the differential phosphorylation, gene ontology annotations were retrieved for the differential phosphoproteins. The results revealed that cell signaling pathway members such as calmodulin and 14‐3‐3 proteins were regulated in response to 24‐h salt stress. Multiple putative salt‐responsive phosphoproteins seem to be involved in the regulation of photosynthesis‐related processes. These results may help to understand the salt‐inducible phosphorylation processes of maize leaves.