Open AccessAcetylation is the most abundant actin modification in Entamoeba histolytica and modifications of actin's amino‐terminal domain change cytoskeleton activities
Author(s) -
HernándezCuevas Nora Adriana,
Jhingan Gagan Deep,
Petropolis Debora,
Vargas Miguel,
Guillen Nancy
Publication year - 2019
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12983
Subject(s) - entamoeba histolytica , biology , acetylation , actin , actin cytoskeleton , cytoskeleton , microbiology and biotechnology , actin binding protein , profilin , actin remodeling , biochemistry , cell , genetics , gene
Actin is one of the most conserved, abundant, and ubiquitous proteins in all eukaryotes characterised to date. Posttranslation modifications of actin modify the organisation of the actin‐rich cytoskeleton. In particular, chemical modifications of actin's amino‐terminal region determine how filamentous actin is organised into scaffolds. After assuming that protein modifications account for the multiple functional activities exerted by the single actin in Entamoeba histolytica , we profiled posttranslational modifications of this protein. Acetylation (on 21 different amino acids) was the most abundant modification, followed by phosphorylation. Furthermore, the glycine residue at Position 2 in E. histolytica 's actin (Gly2, not found in most other eukaryotic actins) was found to be acetylated. The impact of Gly2 on the amoeba's life cycle and pathogenicity was then assessed in mutagenesis experiments. We found that Gly2 was necessary for cell morphology and division, parasite–host cell adhesion, and host invasion in an in vitro model of amoebic human infection.