Analysis of lysine acetylation in tomato spot wilt virus infection in Nicotiana benthamiana

IntroductionKac is a model for all acylation modification studies. Kac plays a critical role in eukaryotes and prokaryotes. It is mainly involved in six major biological functions: gene expression, signal transduction, cell development, protein conversion, metabolism, and metabolite transport. MethodWe investigated and compared the acetylation modification of proteins in healthy and tomato spot wilt virus (TSWV)-infected Nicotiana benthamiana leaves. ResultWe identified 3,418 acetylated lysine sites on 1962 proteins acetylation of proteins in the TSWV-infected and control groups were compared; it was observed that 408 sites on 294 proteins were upregulated and 284 sites on 219 proteins (involved in pentose phosphate, photosynthesis, and carbon fixation in photosynthesis) were downregulated after the infection. Overall, 35 conserved motifs were identified, of which xxxkxxxxx_K_ Rxxxxxxxxx represented 1,334 (31.63%) enrichment motifs and was the most common combination. Bioinformatic analysis revealed that most of the proteins with Kac sites were located in the chloroplast and cytoplasm. They were involved in biological processes, such as cellular and metabolic processes. DiscussionIn conclusion, our results revealed that Kac may participate in the regulation of TSWV infection in N. benthamiana.

Automated summary

Kac is a model for all acylation modification studies and is involved in six major biological functions. In this study, we investigated the acetylation modification of proteins in healthy and TSWV-infected N. benthamiana leaves. Our results showed that acetylation of proteins was significantly altered after the infection, with upregulated and downregulated sites. We also identified conserved motifs and found that most of the Kac proteins were located in the chloroplast and cytoplasm, participating in cellular and metabolic processes.