Comprehensive analysis of protein acetyltransferases of human pathogen Mycobacterium tuberculosis

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.

CircMMP11 regulates proliferation, migration, invasion, and apoptosis of breast cancer cells through miR-625-5p/ZEB2 axis

“…Here, we demonstrated that miR-625-5p targeted ZEB2 in BC cells. Of course, other miRNAs could interact ZEB2 to regulate the occurrence and progression of BC; multiple miRNAs, including miR-30a [ 21 ], miR-653 [ 22 ], miR-448 [ 23 ], and miR-124 [ 24 ] were identified to bind to the 3′UTR of ZEB2 in BC cells.…”

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

“…The diversity of protein functions is facilitated by PTM that changes the structure/function relationship and affects the formation of protein complexes, enzyme catalysis, and other biomolecular interactions ( Cain et al, 2014 ). In recent years, accumulating evidence indicates that PTMs play a critical role in various physiological processes, such as immunometabolism ( Diskin et al, 2020 ), protein synthesis and turnover ( Rioseras et al, 2018 ), protein stability ( Ishigaki et al, 2017 ; Sang et al, 2017 ), dormancy ( Yang et al, 2018 ), nitrogen metabolism ( Macek et al, 2019 ), and virulence ( Xie et al, 2019 ). Among the hundreds of diverse PTMs, protein phosphorylation, acetylation, succinylation, pupylation and ubiquitin-like modifications, glycosylation, and lipidation play a major role in regulating bacterial cell cycle, cell metabolism, persistence, and virulence ( Ren et al, 2016 , 2019 ; Macek et al, 2019 ).…”

First comprehensive analysis of lysine succinylation in paper mulberry (Broussonetia papyrifera)

“…Hundreds of succinylation sites and proteins have been identified in a variety of microorganisms. Various bacteria [ 23 ] and fungi, such as Escherichia coli , Mycobacterium tuberculosis and Toxoplasma gondii , have been shown to undergo succinylation [ 24 , 25 ]. A systematic analysis of mammalian succinylation sites in mouse cells [ 26 ] indicated that protein succinylation sites may affect enzymes involved in mitochondrial metabolism.…”