Proteome-wide identification of lysine succinylation in thermophilic and mesophilic bacteria

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• 作者：Hiroki Okanishi^a ; ^b ; ¹ ; Kwang Kim^a ; ^{kwangkim0169@gmail.com} ; ^{kwangkim@bio.sci.osaka-u.ac.jp} ; Kenji Fukui^c ; Takato Yano^c ; Seiki Kuramitsu^a ; Ryoji Masui^a ; ^b
• 关键词：COGs ; Clusters of orthologous groups ; KAT ; lysine acyltransferase ; KDAC ; lysine deacylase ; LC-MS/MS ; liquid chromatography-tandem mass spectrometry ; PBS ; phosphate buffered saline ; PDB ; Protein Data Bank ; PTM ; post-translational modification ; RCSB ; Research Collaboratory for Structural Bioinformatics
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1865
• 期：2
• 页码：232-242
• 全文大小：1339 K
• 卷排序：1865

文摘

Antibody-based LC-MS/MS identified Lys succinylation sites in five bacterial species. Succinylation events are commonly found in thermophiles as well as mesophiles. Many succinylation sites were located at positions important for protein functions. Dozens of succinylation sites are conserved in different bacteria. The roles of Lys succinylation may differ from those of Lys propionylation.