In-depth proteome analysis reveals multiple pathways involved in tomato SlMPK1-mediated high-temperature responses

• Published in: Protoplasma Vol. 257; no. 1; pp. 43 - 59
• Main Authors: Ding, Haidong, Wu, Yuan, Yuan, Guibo, Mo, Shuangrong, Chen, Qi, Xu, Xiaoying, Wu, Xiaoxia, Ge, Cailin
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 2020; Springer Nature B.V
• Subjects: Amino acids; Biomedical and Life Sciences; Cell Biology; Environmental factors; Environmental stress; High temperature; Kinases; Life Sciences; MAP kinase; Original Article; Oxidation; Photosynthesis; Plant Sciences; Protein folding; Protein kinase; Proteolysis; Proteomes; Quantitation; Ribonucleic acid; RNA; RNA-mediated interference; Zoology; iTRAQ-based proteome; High temperature; Tomato; MAP kinase 1
• ISSN: 0033-183X; 1615-6102
• DOI: 10.1007/s00709-019-01419-6

High temperature (HT) is one of the major environmental factors which limits plant growth and yield. The mitogen-activated protein kinase (MAPK) plays vital roles in environmental stress responses. However, the mechanisms triggered by MAPKs in plants in response to HT are still extremely limited. In this study, the proteomic data of differences between SlMPK1 RNA-interference mutant (SlMPK1i) and wild type and of tomato ( Solanum lycopersicum ) plants under HT stress using isobaric tags for relative and absolute quantitation (iTRAQ) was re-analyzed in depth. In total, 168 differently expressed proteins (DEPs) were identified in response to HT stress, including 38 DEPs only found in wild type, and 84 DEPs specifically observed in SlMPK1i after HT treatment. The majority of higher expression of 84 DEPs were annotated into photosynthesis, oxidation-reduction process, protein folding, translation, proteolysis, stress response, and amino acid biosynthetic process. More importantly, SlMPK1-mediated photosynthesis was confirmed by the physiological characterization of SlMPK1i with a higher level of photosynthetic capacity under HT stress. Overall, the results reveal a set of potential candidate proteins helping to further understand the intricate regulatory network regulated by SlMPK1 in response to HT.