Intracellular Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii DL1

BMC Microbiology

Zoltan Blum¹  Gunnel Svensäter²  Carolina Robertsson²  Claes Wickström² 

[1] Department of Biomedical Science, Malmö University, 20506, Malmö, Sweden;Department of Oral Biology and Pathology, Faculty of Odontology, Malmö University, 20506, Malmö, Sweden;

关键词: 2DE;    Oral bacteria;    Phosphoproteome;    Pro-Q diamond;    Streptococci;    Streptococcus gordonii;   

DOI  :  10.1186/s12866-020-01944-y

来源: Springer

【 摘 要 】

BackgroundTo respond and adapt to environmental challenges, prokaryotes regulate cellular processes rapidly and reversibly through protein phosphorylation and dephosphorylation. This study investigates the intracellular proteome and Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii. Intracellular proteins from planktonic cells of S. gordonii DL1 were extracted and subjected to 2D-gel electrophoresis. Proteins in general were visualized using Coomassie Brilliant Blue and T-Rex staining. Phosphorylated proteins were visualized with Pro-Q Diamond Phosphoprotein Gel Stain. Proteins were identified by LC-MS/MS and sequence analysis.ResultsIn total, sixty-one intracellular proteins were identified in S. gordonii DL1, many of which occurred at multiple isoelectric points. Nineteen of these proteins were present as one or more Ser/Thr/Tyr phosphorylated form. The identified phosphoproteins turned out to be involved in a variety of cellular processes.ConclusionNineteen phosphoproteins involved in various cellular functions were identified in S. gordonii. This is the first time the global intracellular Ser/Thr/Tyr phosphorylation profile has been analysed in an oral streptococcus. Comparison with phosphoproteomes of other species from previous studies showed many similarities. Proteins that are consistently found in a phosphorylated state across several species and growth conditions may represent a core phosphoproteome profile shared by many bacteria.

【 授权许可】

CC BY