ArticleMicrobiologyOpen2020
Acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens.
Article in MicrobiologyOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Acetyl-Phosphate Dependent Protein Acetylation in Neisseria gonorrhoeae.MicrobiologyOpen · 2026Article
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
- Widespread Involvement of Acetylation in the Retinal Metabolism of Form-Deprivation Myopia in Guinea Pigs.ACS omega · 2023Article
- Holistic analysis of lysine acetylation in aquaculture pathogenic bacteriaFrontiers in veterinary science · 2023Article
- Article
- A Comprehensive Analysis of the Lysine Acetylome in the Aquatic Animals Pathogenic BacteriumFrontiers in microbiology · 2022Article
- Acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens.MicrobiologyOpen · 2020Article
- Genome- and Proteome-Wide Analysis of Lysine Acetylation inFrontiers in microbiology · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein lysine acetylation, a dynamic and reversible posttranslational modification, plays a crucial role in several cellular processes, including cell cycle regulation, metabolism, enzymatic activities, and protein interactions. Brenneria nigrifluens is a pathogen of walnut trees with shallow bark canker and can cause serious disease in walnut trees. Until now, a little has been known about the roles of lysine acetylation in plant pathogenic bacteria. In the present study, the lysine acetylome of B. nigrifluens was determined by high-resolution LC-MS/MS analysis. In total, we identified 1,866 lysine acetylation sites distributed in 737 acetylated proteins. Bioinformatics results indicated that acetylated proteins participate in many different biological functions in B. nigrifluens. Four conserved motifs, namely, LK
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Registered trials
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