Curated Papers > In recent years, high-impact research on "synthetic biology" (IF≥30, last 5 years)

Protein post-translational modifications in bacteria.

Literature Information

DOI	10.1038/s41579-019-0243-0
PMID	31485032
Journal	Nature reviews. Microbiology
Impact Factor	103.3
JCR Quartile	Q1
Publication Year	2019
Times Cited	183
Keywords	Protein post-translational modifications, Bacteria, Cellular processes
Literature Type	Journal Article, Research Support, Non-U.S. Gov't, Review
ISSN	1740-1526
Pages	651-664
Issue	17(11)
Authors	Boris Macek, Karl Forchhammer, Julie Hardouin, Eilika Weber-Ban, Christophe Grangeasse, Ivan Mijakovic

TL;DR

This study highlights the increasing recognition of protein post-translational modifications (PTMs) in bacteria, which, although occurring at lower frequencies than in eukaryotes, play crucial roles in cellular processes such as protein synthesis, metabolism, and virulence. Understanding these modifications can enhance our knowledge of bacterial physiology and potentially lead to new treatments for infectious diseases.

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Protein post-translational modifications · Bacteria · Cellular processes

Abstract

Over the past decade the number and variety of protein post-translational modifications that have been detected and characterized in bacteria have rapidly increased. Most post-translational protein modifications occur in a relatively low number of bacterial proteins in comparison with eukaryotic proteins, and most of the modified proteins carry low, substoichiometric levels of modification; therefore, their structural and functional analysis is particularly challenging. The number of modifying enzymes differs greatly among bacterial species, and the extent of the modified proteome strongly depends on environmental conditions. Nevertheless, evidence is rapidly accumulating that protein post-translational modifications have vital roles in various cellular processes such as protein synthesis and turnover, nitrogen metabolism, the cell cycle, dormancy, sporulation, spore germination, persistence and virulence. Further research of protein post-translational modifications will fill current gaps in the understanding of bacterial physiology and open new avenues for treatment of infectious diseases.

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Primary Questions Addressed

1. What specific types of post-translational modifications are most commonly observed in bacterial proteins, and how do they compare to those in eukaryotes?
2. How do environmental factors influence the extent and types of post-translational modifications in different bacterial species?
3. What role do modifying enzymes play in the regulation of bacterial protein function, and how does this vary across species?
4. In what ways do protein post-translational modifications impact bacterial virulence and persistence in host organisms?
5. What methodologies are currently being developed or improved to study the structural and functional implications of post-translational modifications in bacteria?

Key Findings

Key Insights on Protein Post-Translational Modifications in Bacteria

1. Research Background and Objectives

The study of protein post-translational modifications (PTMs) in bacteria has gained significant momentum over the last decade. Historically, research in this area lagged behind that of eukaryotic systems, which are known for a wide array of PTMs. However, recent advancements have led to the identification and characterization of various PTMs in bacteria, revealing their potential importance in diverse biological processes. The primary objective of this research is to elucidate the role of PTMs in bacterial physiology, particularly how these modifications impact protein functionality and cellular processes.

2. Main Methods and Findings

The research utilized various biochemical and analytical techniques to detect and characterize PTMs in bacterial proteins. Despite the increasing discovery of PTMs, it is noted that these modifications occur in a relatively small subset of bacterial proteins compared to eukaryotes. Moreover, many bacterial proteins exhibit low, substoichiometric levels of modification, presenting challenges for structural and functional analysis. The study highlights significant variability in the number and types of modifying enzymes across different bacterial species, indicating that the modified proteome is highly contingent on environmental conditions. The findings demonstrate that PTMs play crucial roles in multiple cellular processes, including protein synthesis, nitrogen metabolism, cell cycle regulation, dormancy, sporulation, spore germination, persistence, and virulence.

3. Core Conclusions

The research concludes that protein post-translational modifications are indispensable for the functional versatility of bacterial proteins. Despite their low abundance and the limited number of proteins that undergo modification, PTMs are integral to essential cellular functions and adaptations in response to environmental stimuli. The disparity in modifying enzymes among bacterial species suggests a tailored approach to understanding bacterial physiology and adaptation mechanisms.

4. Research Significance and Impact

This study significantly enriches the current understanding of bacterial biology by highlighting the underappreciated role of PTMs. As bacteria are pivotal in various ecological and pathogenic contexts, elucidating the mechanisms of PTMs can provide insights into bacterial behavior, resilience, and virulence. This understanding is crucial for developing novel therapeutic strategies to combat bacterial infections and enhance the efficacy of existing treatments. By identifying PTM-related pathways, researchers can potentially target these modifications to mitigate bacterial pathogenicity or enhance beneficial bacterial functions in industrial and environmental applications. Overall, this research paves the way for future investigations into bacterial physiology and the development of innovative approaches to address microbial challenges.

Literatures Citing This Work

1. Substrate recognition by the Pseudomonas aeruginosa EF-Tu-modifying methyltransferase EftM. - Emily G Kuiper;Debayan Dey;Paige A LaMore;Joshua P Owings;Samantha M Prezioso;Joanna B Goldberg;Graeme L Conn - The Journal of biological chemistry (2019)
2. Small-Molecule Acetylation by GCN5-Related N-Acetyltransferases in Bacteria. - Rachel M Burckhardt;Jorge C Escalante-Semerena - Microbiology and molecular biology reviews : MMBR (2020)
3. Aminoacyl-tRNA synthetases. - Miguel Angel Rubio Gomez;Michael Ibba - RNA (New York, N.Y.) (2020)
4. Expression of actively soluble antigen-binding fragment (Fab) antibody and GFP fused Fab in the cytoplasm of the engineered Escherichia coli. - Supaluk Krittanai;Waraporn Putalun;Seiichi Sakamoto;Hiroyuki Tanaka;Thaweesak Juengwatanatrakul;Gorawit Yusakul - Molecular biology reports (2020)
5. The Involvement of the McsB Arginine Kinase in Clp-Dependent Degradation of the MgsR Regulator in Bacillus subtilis. - Lars Lilge;Alexander Reder;Frank Tippmann;Friedrich Morgenroth;Janice Grohmann;Dörte Becher;Katharina Riedel;Uwe Völker;Michael Hecker;Ulf Gerth - Frontiers in microbiology (2020)
6. Open Database Searching Enables the Identification and Comparison of Bacterial Glycoproteomes without Defining Glycan Compositions Prior to Searching. - Ameera Raudah Ahmad Izaham;Nichollas E Scott - Molecular & cellular proteomics : MCP (2020)
7. Regulation of Protein Post-Translational Modifications on Metabolism of Actinomycetes. - Chen-Fan Sun;Yong-Quan Li;Xu-Ming Mao - Biomolecules (2020)
8. The Role of Proteomics in Bacterial Response to Antibiotics. - Foteini Tsakou;Rosa Jersie-Christensen;Håvard Jenssen;Biljana Mojsoska - Pharmaceuticals (Basel, Switzerland) (2020)
9. The Phage-Encoded N-Acetyltransferase Rac Mediates Inactivation of Pseudomonas aeruginosa Transcription by Cleavage of the RNA Polymerase Alpha Subunit. - Pieter-Jan Ceyssens;Jeroen De Smet;Jeroen Wagemans;Natalia Akulenko;Evgeny Klimuk;Subray Hedge;Marleen Voet;Hanne Hendrix;Jan Paeshuyse;Bart Landuyt;Hua Xu;John Blanchard;Konstantin Severinov;Rob Lavigne - Viruses (2020)
10. Exoproteomics for Better Understanding Pseudomonas aeruginosa Virulence. - Salomé Sauvage;Julie Hardouin - Toxins (2020)

... (173 more literatures)

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