35 research outputs found
Molecular gut content analysis demonstrates that Calanus grazing on Phaeocystis pouchetii and Skeletonema marinoi is sensitive to bloom phase but not prey density
Integrative testis transcriptome analysis reveals differentially expressed miRNAs and their mRNA targets during early puberty in Atlantic salmon
Proteomic and bioinformatic pipeline to screen the ligands of S. pneumoniae interacting with human brain microvascular endothelial cells
Proteome-wide Lysine Glutarylation Profiling of the <i>Mycobacterium tuberculosis</i> H37Rv
Lysine
glutarylation, a new protein posttranslational modification
(PTM), was recently identified and characterized in both prokaryotic
and eukaryotic cells. To explore the distribution of lysine glutarylation
in <i>Mycobacterium tuberculsosis</i>, by using a comprehensive
method combining the immune affinity peptide enrichment by the glutaryl-lysine
antibody with LCâMS, we finally identified 41 glutarylation
sites in 24 glutarylated proteins from <i>M. tuberculosis</i>. These glutarylated proteins are involved in various cellular functions
such as translation and metabolism and exhibit diverse subcellular
localizations. Three common glutarylated proteins including 50S ribosomal
protein L7/L12, elongation factor Tu, and dihydrolipoamide succinyltransferase
are shared between <i>Escherichia coli</i> and <i>M. tuberculosis</i>. Moreover, comparison with other PTMs characterized in <i>M. tuberculosis</i>, 15 glutarylated proteins, are found to be both acetylated and succinylated.
Notably, several stress-response-associated proteins including HspX
are glutarylated. Our data provide the first analysis of <i>M. tuberculosis</i> lysine glutarylated proteins. Further studies on the role of the
glutarylated proteins will unveil the molecular mechanisms of glutarylation
underlying <i>M. tuberculosis</i> physiology and pathogenesis