Global profiling of lysine acetylation in human histoplasmosis pathogen Histoplasma capsulatum

The International Journal of Biochemistry & Cell Biology
Longxiang XieWeihua Pan

Abstract

Histoplasma capsulatum is the causative agent of human histoplasmosis, which can cause respiratory and systemic mycosis in immune-compromised individuals. Lysine acetylation, a protein posttranslational protein modification, is widespread in both eukaryotes and prokaryotes. Although increasing evidence suggests that lysine acetylation may play critical roles in fungus physiology, very little is known about its extent and function in H. capsulatum. To comprehensively profile protein lysine acetylation in H. capsulatum, we performed a global acetylome analysis through peptide prefractionation, antibody enrichment, and LC-MS/MS analysis, identifying 775 acetylation sites on 456 acetylated proteins; and functionally analysis showing their involvement in different biological processes. We defined six types of acetylation site motifs, and the results imply that lysine residue of polypeptide with tyrosine at the -1 and +1 positions, histidine at the +1 position, and phenylalanine (F) at the +1 and +2 position is a preferred substrate of lysine acetyltransferase. Moreover, some virulence factors candidates including calmodulin and DnaK are acetylated. In conclusion, our data set may serve as an important resource for the elucidation of...Continue Reading

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Citations

Sep 7, 2018·Plant, Cell & Environment·Sotirios FragkostefanakisKlaus-Dieter Scharf
Oct 26, 2018·Molecular Ecology Resources·Antton AlberdiMarcus Thomas Pius Gilbert
Mar 15, 2020·Brazilian Journal of Microbiology : [publication of the Brazilian Society for Microbiology]·Natália Sayuri WassanoAndré Damasio
Nov 3, 2020·Frontiers in Microbiology·Junzhu ChenXiaotian Huang

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