Proteome-Wide Identification of Lysine Succinylation in the Proteins of Tomato (Solanum lycopersicum).
Proteome-Wide Identification of Lysine Succinylation in the Proteins of Tomato (Solanum lycopersicum).
复制标题
番茄(Solanum lycopersicum)蛋白质中赖氨酸琥珀酰化的全蛋白质组鉴定
DOI:
10.1371/journal.pone.0147586
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发表时间:
2016
期刊:
影响因子:
3.7
通讯作者:
Wu F
中科院分区:
文献类型:
--
作者:
Jin W;Wu F
Post-translational modification of proteins through lysine succinylation plays important regulatory roles in living cells. Lysine succinylation was recently identified as a novel post-translational modification in Escherichia coli, yeast, Toxoplasma gondii, HeLa cells, and mouse liver. Interestingly, only a few sites of lysine succinylation have been detected in plants to date. In this study, we identified 347 sites of lysine succinylation in 202 proteins in tomato by using high-resolution mass spectrometry. Succinylated proteins are implicated in the regulation of diverse metabolic processes, including chloroplast and mitochondrial metabolism. Bioinformatic analysis showed that succinylated proteins are evolutionarily conserved and involved in various cellular functions such as metabolism and epigenetic regulation. Moreover, succinylated proteins exhibit diverse subcellular localizations. We also defined six types of definitively conserved succinylation motifs. These results provide the first in-depth analysis of the lysine succinylome and novel insights into the role of succinylation in tomato, thereby elucidating lysine succinylation in the context of cellular physiology and metabolite biosynthesis in plants.