ArticlePloS one2015
Site-Specific Ser/Thr/Tyr Phosphoproteome of Sinorhizobium meliloti at Stationary Phase.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Phosphomimetic mutations near active sites of proteins in Thermus thermophilus suggest a widespread regulatory mechanism.FEBS open bio · 2025Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- Addressing the Possibility of a Histone-Like Code in Bacteria.Journal of proteome research · 2021Review
- Comparative Phosphoproteomics of Classical Bordetellae Elucidates the Potential Role of Serine, Threonine and Tyrosine Phosphorylation inFrontiers in cellular and infection microbiology · 2021Article
- Evolutionary Rescue of an EnvironmentalFrontiers in microbiology · 2020Article
- Article
- Goals and Challenges in Bacterial Phosphoproteomics.International journal of molecular sciences · 2019Review
- Mutation in theGenes · 2018Article
- Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance.BMC microbiology · 2017Article
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Authors and funding
3 authors.
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Abstract
Sinorhizobium meliloti, a facultative microsymbiont of alfalfa, should fine-tune its cellular processes to live saprophytically in soils characterized with limited nutrients and diverse stresses. In this study, TiO2 enrichment and LC-MS/MS were used to uncover the site-specific Ser/Thr/Tyr phosphoproteome of S. meliloti in minimum medium at stationary phase. There are a total of 96 unique phosphorylated sites, with a Ser/Thr/Tyr distribution of 63:28:5, in 77 proteins. Phosphoproteins identified in S. meliloti showed a wide distribution pattern regarding to functional categories, such as replication, transcription, translation, posttranslational modification, transport and metabolism of amino acids, carbohydrate, inorganic ion, succinoglycan etc. Ser/Thr/Tyr phosphosites identified within the conserved motif in proteins of key cellular function indicate a crucial role of phosphorylation in modulating cellular physiology. Moreover, phosphorylation in proteins involved in processes related to rhizobial adaptation was also discussed, such as those identified in SMa0114 and PhaP2 (polyhydroxybutyrate synthesis), ActR (pH stress and microaerobic adaption), SupA (potassium stress), chaperonin GroEL2 (viability and potentially symbiosis), and ExoP (succinoglycan synthesis and secretion). These Ser/Thr/Tyr phosphosites identified herein would be helpful for our further investigation and understanding of the role of phosphorylation in rhizobial physiology.
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