ArticleBioscience reports2019
Comprehensive analysis of protein acetyltransferases of human pathogen Mycobacterium tuberculosis.
Article in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- The Pyridoxal-5'-Phosphate-Dependent Enzymes ofACS infectious diseases · 2026Review
- The acetyltransferase CysE modulates virulence and drug resistance of Mycobacterium tuberculosis by interfering with oxidative stress responses.Communications biology · 2025Article
- The role ofFrontiers in cellular and infection microbiology · 2023Review
- Article
- A Comprehensive Analysis of the Lysine Acetylome in the Aquatic Animals Pathogenic BacteriumFrontiers in microbiology · 2022Article
- Predicting circRNA-Disease Associations Based on Deep Matrix Factorization with Multi-source Fusion.Interdisciplinary sciences, computational life sciences · 2021Article
- First comprehensive analysis of lysine succinylation in paper mulberry (Broussonetia papyrifera).BMC genomics · 2021Article
- Regulation of Protein Post-Translational Modifications on Metabolism of Actinomycetes.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tuberculosis (TB), a leading infectious disease caused by Mycobacterium tuberculosis strain, takes four human lives every minute globally. Paucity of knowledge on M. tuberculosis virulence and antibiotic resistance is the major challenge for tuberculosis control. We have identified 47 acetyltransferases in the M. tuberculosis, which use diverse substrates including antibiotic, amino acids, and other chemical molecules. Through comparative analysis of the protein file of the virulent M. tuberculosis H37Rv strain and the avirulent M. tuberculosis H37Ra strain, we identified one acetyltransferase that shows significant variations with N-terminal deletion, possibly influencing its physicochemical properties. We also found that one acetyltransferase has three types of post-translation modifications (lysine acetylation, succinylation, and glutarylation). The genome context analysis showed that many acetyltransferases with their neighboring genes belong to one operon. By data mining from published transcriptional profiles of M. tuberculosis exposed to diverse treatments, we revealed that several acetyltransferases may be functional during M. tuberculosis infection. Insights obtained from the present study can potentially provide clues for developing novel TB therapeutic interventions.
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