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.

journal_name

Biosci Rep

journal_title

Bioscience reports

authors

Xie L,Yang W,Fan X,Xie J

doi

10.1042/BSR20191661

subject

Has Abstract

pub_date

2019-12-20 00:00:00

issue

12

eissn

0144-8463

issn

1573-4935

pii

221456

journal_volume

39

pub_type

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