Acetylome analysis of lysine acetylation in the plant pathogenic bacterium <i>Brenneria nigrifluens</i>

Li, Yong; Han, Xue; Bian, Dan-Ran; Xu, Guan‐tang; Piao, Chun‐gen

doi:10.1002/mbo3.952

Cited by 9 publications

(8 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Of the 1,924 acetylated proteins, 65.80% contain two or more acetylation sites, and 4.47% contain more than 10 acetylation sites ( Figure 4B ). This proportion is also slightly higher than that found in previous studies ( Jers et al, 2017 ; Li et al, 2020 ; Pang et al, 2020 ), while further experiments are required to validate these acetylated proteins in the future. We further determined the frequencies of amino acids around the acetylated lysine site ( Supplementary Table S6 and Supplementary Figure S6 ).…”

Section: Resultscontrasting

confidence: 62%

“…found in previous studies (Jers et al, 2017;Li et al, 2020;Pang et al, 2020), while further experiments are required to validate these acetylated proteins in the future. We further determined the frequencies of amino acids around the acetylated lysine site ( Supplementary Table S6 and Supplementary Figure S6).…”

Section: Comprehensive Analysis Of Lysine Acetylated Proteins In V Vmentioning

confidence: 64%

See 1 more Smart Citation

Genome- and Proteome-Wide Analysis of Lysine Acetylation in Vibrio vulnificus Vv180806 Reveals Its Regulatory Roles in Virulence and Antibiotic Resistance

et al. 2020

View full text Add to dashboard Cite

Infection with Vibrio vulnificus is notorious for its atypical clinical manifestations and irreversible disease progression. Lysine acetylation is a conserved post-translational modification (PTM) that plays a critical regulatory role in diverse cellular processes. However, little is known about the role of lysine acetylation on the pathogenesis of V. vulnificus. Here, we report the complete genome sequence and a global profile for protein lysine acetylation of V. vulnificus Vv180806, a highly cefoxitin resistant strain isolated from a mortality case. The assembled genome comprised two circular chromosomes and one circular plasmid; it contained 4,770 protein-coding genes and 153 RNA genes. Phylogenetic analysis revealed genetic homology of this strain with other V. vulnificus strains from food sources. Of all the proteins in this strain, 1,924 (40.34%) were identified to be acetylated at 6,626 sites. The acetylated proteins were enriched in metabolic processes, binding functions, cytoplasm, and multiple central metabolic pathways. Moreover, the acetylation was found in most identified virulence factors of this strain, suggesting its potentially important role in bacterial virulence. Our work provides insights into the genomic and acetylomic features responsible for the virulence and antibiotic resistance of V. vulnificus, which will facilitate future investigations on the pathogenesis of this bacterium.

show abstract

Section: Resultscontrasting

confidence: 62%

Section: Comprehensive Analysis Of Lysine Acetylated Proteins In V Vmentioning

confidence: 64%

Genome- and Proteome-Wide Analysis of Lysine Acetylation in Vibrio vulnificus Vv180806 Reveals Its Regulatory Roles in Virulence and Antibiotic Resistance

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Motif K ac R has been reported in other species of bacteria and plants, such as Streptococcus pneumoniae , Vibrio cholerae , Cyanobacterium Synechocystis sp., wheat ( Triticum aestivum L.), and Zea mays ( Mo et al, 2015 ; Carsten et al, 2017 ; Liu et al, 2018 ; Guo et al, 2020 ; Yan et al, 2020 ), indicating that the K ac R motif is conserved and widespread. Motif K ac L and L.K ac have been reported in Brenneria nigrifluens ( Li Y. et al, 2020 ). The other motifs, LK ac K, L(-7) EK ac K, and IEK ac , are rarely identified in other bacteria.…”

Section: Resultsmentioning

confidence: 94%

A Comprehensive Analysis of the Lysine Acetylome in the Aquatic Animals Pathogenic Bacterium Vibrio mimicus

et al. 2022

View full text Add to dashboard Cite

Protein lysine acetylation is an evolutionarily conserved post-translational modification (PTM), which is dynamic and reversible, playing a crucial regulatory role in almost every aspect of metabolism, of both eukaryotes and prokaryotes. Several global lysine acetylome studies have been carried out in various bacteria, but thus far, there have been no reports of lysine acetylation for the commercially important aquatic animal pathogen Vibrio mimicus. In the present study, we used anti-Ac-K antibody beads to highly sensitive immune-affinity purification and combined high-resolution LC-MS/MS to perform the first global lysine acetylome analysis in V. mimicus, leading to the identification of 1,097 lysine-acetylated sites on 582 proteins, and more than half (58.4%) of the acetylated proteins had only one site. The analysis of acetylated modified peptide motifs revealed six significantly enriched motifs, namely, KacL, KacR, L(-2) KacL, LKacK, L(-7) EKac, and IEKac. In addition, bioinformatic assessments state clearly that acetylated proteins have a hand in many important biological processes in V. mimicus, such as purine metabolism, ribosome, pyruvate metabolism, glycolysis/gluconeogenesis, the TCA cycle, and so on. Moreover, 13 acetylated proteins were related to the virulence of V. mimicus. To sum up, this is a comprehensive analysis whole situation protein lysine acetylome in V. mimicus and provides an important foundation for in-depth study of the biological function of lysine acetylation in V. mimicus.

show abstract

“…The discovery here that acetylation of one specific lysine residue in FolSvp1 increases the stability of this protein in Fol and in planta, promoting invasion of tomato, provides a clear example of a direct effect of acetylation on a biological process in plant pathogens. With the recent discovery that a large number of putative effectors are acetylated in fungi ( Li et al, 2020a , Lv et al, 2016 ; Zhou et al, 2016 ), Phytophthora ( Li et al, 2016 ), and bacteria ( Li et al, 2020b , Ren et al, 2017 ), it is likely that the findings reported here are only the beginning of what will be a widespread phenomenon in plant pathogens.…”

Section: Discussionmentioning

confidence: 94%

Acetylation of a fungal effector that translocates host PR1 facilitates virulence

Wang

et al. 2022

eLife

View full text Add to dashboard Cite

Pathogens utilize a panoply of effectors to manipulate plant defense. However, despite their importance, relatively little is actually known about regulation of these virulence factors. Here, we show that the effector FolSvp1, secreted from fungal pathogen Fusarium oxysporum f. sp. lycopersici (Fol) directly binds and translocates the tomato pathogenesis-related protein1, SlPR1, from the apoplast outside the plasma membrane to the host nucleus via its nuclear localization signal. Relocation of SlPR1 abolishes generation of the defense signaling peptide, CAPE1, from its C-terminus, and as a consequence, facilitates pathogen invasion of plants. The action of FolSvp1 requires covalent modification by acetylation for full virulence in host tomato tissues. The modification is catalyzed by the Fol FolArd1 lysine acetyltransferase prior to secretion. Addition of an acetyl group to one residue, K167, prevents ubiquitination-dependent degradation of FolSvp1 in both Fol and plant cells with different mechanisms, allowing it to function normally in fungal invasion. Either inactivation of FolSvp1 or removal of the acetyl group on K167 leads to impaired pathogenicity of Fol. These findings indicate that acetylation can regulate the stability of effectors of fungal plant pathogens with impact on virulence.

show abstract

Acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens

Cited by 9 publications

References 47 publications

Genome- and Proteome-Wide Analysis of Lysine Acetylation in Vibrio vulnificus Vv180806 Reveals Its Regulatory Roles in Virulence and Antibiotic Resistance

Genome- and Proteome-Wide Analysis of Lysine Acetylation in Vibrio vulnificus Vv180806 Reveals Its Regulatory Roles in Virulence and Antibiotic Resistance

A Comprehensive Analysis of the Lysine Acetylome in the Aquatic Animals Pathogenic Bacterium Vibrio mimicus

Acetylation of a fungal effector that translocates host PR1 facilitates virulence

Contact Info

Product

Resources

About