title: Proteome-Wide Identification of Lysine Succinylation in the Proteins of Tomato (Solanum lycopersicum).
abstract: 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.
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Weibo
authors.initials: W
authors.lastname: Jin
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Fangli
authors.initials: F
authors.lastname: Wu
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D002952:Citric Acid Cycle; D063990:Gene Ontology; D006657:Histones / Q000378:metabolism; D018551:Solanum lycopersicum / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D021381:Protein Transport; D020543:Proteome / Q000378:metabolism*; D013045:Species Specificity; D013347:Subcellular Fractions / Q000378:metabolism; D019802:Succinic Acid / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
chemical_list: D006657:Histones; D010455:Peptides; D010940:Plant Proteins; D020543:Proteome; D019802:Succinic Acid; D008239:Lysine
references.citation: Science. 2009 Aug 14;325(5942):834-40
references.pmid: 19608861
references.citation: Curr Opin Plant Biol. 2007 Dec;10(6):645-52
references.pmid: 17884714
references.citation: Plant J. 2011 Apr;66(1):4-17
references.pmid: 21443619
references.citation: Cell. 2011 Oct 14;147(2):263-6
references.pmid: 22000006
references.citation: Science. 2011 Nov 11;334(6057):806-9
references.pmid: 22076378
references.citation: Mol Cell Proteomics. 2011 Dec;10(12):M111.012658
references.pmid: 21908771
references.citation: Mol Cell Proteomics. 2012 May;11(5):100-7
references.pmid: 22389435
references.citation: ACS Chem Biol. 2012 Jun 15;7(6):947-60
references.pmid: 22571489
references.citation: Cell Rep. 2013 Aug 29;4(4):842-51
references.pmid: 23954790
references.citation: J Proteome Res. 2014 Dec 5;13(12):6087-95
references.pmid: 25377623
references.citation: Annu Rev Biochem. 1998;67:425-79
references.pmid: 9759494
references.citation: Mol Cell. 2006 Aug;23(4):607-18
references.pmid: 16916647
references.citation: Cell. 2007 Feb 23;128(4):693-705
references.pmid: 17320507
references.citation: Nature. 2007 May 24;447(7143):407-12
references.pmid: 17522673
references.citation: Curr Opin Cell Biol. 2007 Jun;19(3):273-80
references.pmid: 17466503
references.citation: Nat Chem Biol. 2011 Jan;7(1):58-63
references.pmid: 21151122