Systematic Analysis of Lysine Acetylation Reveals Diverse Functions in Azorhizobium caulinodans Strain ORS571

Liu, Yanan; Liu, Xiaolin; Dong, Xiaoyan; Yin, Zhiqiu; Xie, Zhihong; Luo, Yongming

doi:10.1128/spectrum.03539-22

Cited by 2 publications

(2 citation statements)

References 87 publications

(123 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…59 Azorhizobium caulinodans contains 2302 acetylation sites on 982 proteins, and as with many bacterial species, acetylated proteins were involved in energy metabolism. 60 In particular, acetylated proteins were enriched in the TCA cycle, ribosomes, metabolism of glycerol and lipids, glucose, pyruvate metabolism, and bacterial chemotaxis. One acetylated protein, the chemotaxis master regulator CheY, was further examined.…”

Section: Understanding Of Lysine Acylations In Bacteriamentioning

confidence: 99%

Recent Contributions of Proteomics to Our Understanding of Reversible N^ε-Lysine Acylation in Bacteria

Popova,

Carr,

Carabetta

2024

J. Proteome Res.

View full text Add to dashboard Cite

Post-translational modifications (PTMs) have been extensively studied in both eukaryotes and prokaryotes. Lysine acetylation, originally thought to be a rare occurrence in bacteria, is now recognized as a prevalent and important PTM in more than 50 species. This expansion in interest in bacterial PTMs became possible with the advancement of mass spectrometry technology and improved reagents such as acyl-modification specific antibodies. In this Review, we discuss how mass spectrometrybased proteomic studies of lysine acetylation and other acyl modifications have contributed to our understanding of bacterial physiology, focusing on recently published studies from 2018 to 2023. We begin with a discussion of approaches used to study bacterial PTMs. Next, we discuss newly characterized acylomes, including acetylomes, succinylomes, and malonylomes, in different bacterial species. In addition, we examine proteomic contributions to our understanding of bacterial virulence and biofilm formation. Finally, we discuss the contributions of mass spectrometry to our understanding of the mechanisms of acetylation, both enzymatic and nonenzymatic. We end with a discussion of the current state of the field and possible future research avenues to explore.

show abstract

Section: Understanding Of Lysine Acylations In Bacteriamentioning

confidence: 99%

Recent Contributions of Proteomics to Our Understanding of Reversible N^ε-Lysine Acylation in Bacteria

Popova,

Carr,

Carabetta

2024

J. Proteome Res.

View full text Add to dashboard Cite

show abstract

“…Mass spectrometry analysis of different bacterial proteomes has identified many acetylation sites on proteins. The functional annotation showed that some of the acetylated proteins are involved in translation and transcription ( Weinert et al., 2013 ; Nakayasu et al., 2017 ; Christensen et al., 2019b ; Marakasova et al., 2020 ; Liu et al., 2023 ).…”

Section: Lysine Acetylation Is Involved In Bacterial Translationmentioning

confidence: 99%

Bacterial protein acetylation: mechanisms, functions, and methods for study

Rizo,

Encarnación-Guevara

2024

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Lysine acetylation is an evolutionarily conserved protein modification that changes protein functions and plays an essential role in many cellular processes, such as central metabolism, transcriptional regulation, chemotaxis, and pathogen virulence. It can alter DNA binding, enzymatic activity, protein-protein interactions, protein stability, or protein localization. In prokaryotes, lysine acetylation occurs non-enzymatically and by the action of lysine acetyltransferases (KAT). In enzymatic acetylation, KAT transfers the acetyl group from acetyl-CoA (AcCoA) to the lysine side chain. In contrast, acetyl phosphate (AcP) is the acetyl donor of chemical acetylation. Regardless of the acetylation type, the removal of acetyl groups from acetyl lysines occurs only enzymatically by lysine deacetylases (KDAC). KATs are grouped into three main superfamilies based on their catalytic domain sequences and biochemical characteristics of catalysis. Specifically, members of the GNAT are found in eukaryotes and prokaryotes and have a core structural domain architecture. These enzymes can acetylate small molecules, metabolites, peptides, and proteins. This review presents current knowledge of acetylation mechanisms and functional implications in bacterial metabolism, pathogenicity, stress response, translation, and the emerging topic of protein acetylation in the gut microbiome. Additionally, the methods used to elucidate the biological significance of acetylation in bacteria, such as relative quantification and stoichiometry quantification, and the genetic code expansion tool (CGE), are reviewed.

show abstract

Systematic Analysis of Lysine Acetylation Reveals Diverse Functions in Azorhizobium caulinodans Strain ORS571

Cited by 2 publications

References 87 publications

Recent Contributions of Proteomics to Our Understanding of Reversible N^ε-Lysine Acylation in Bacteria

Recent Contributions of Proteomics to Our Understanding of Reversible N^ε-Lysine Acylation in Bacteria

Bacterial protein acetylation: mechanisms, functions, and methods for study

Contact Info

Product

Resources

About

Systematic Analysis of Lysine Acetylation Reveals Diverse Functions in Azorhizobium caulinodans Strain ORS571

Cited by 2 publications

References 87 publications

Recent Contributions of Proteomics to Our Understanding of Reversible Nε-Lysine Acylation in Bacteria

Recent Contributions of Proteomics to Our Understanding of Reversible Nε-Lysine Acylation in Bacteria

Bacterial protein acetylation: mechanisms, functions, and methods for study

Contact Info

Product

Resources

About

Recent Contributions of Proteomics to Our Understanding of Reversible N^ε-Lysine Acylation in Bacteria

Recent Contributions of Proteomics to Our Understanding of Reversible N^ε-Lysine Acylation in Bacteria