SUMOylation and deimination of proteins: two epigenetic modifications involved in Giardia encystation

VRANYCH CV; RIVERO MR; MERINO MC; MAYOL, G; ZAMPONI N; MALETTO, BELKYS ANGELICA; PISTORESI MARIA CRISTINA; TOUZ MC; ROPOLO A

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2014 vol. 8

p style="margin: 0cm 0cm 0pt; line-height: 150%;">SUMOylation, a posttranslational modification of proteins, has been recently described as vital in eukaryotic cells. In a previous work, we analyzed the role of SUMO protein and the genes encoding the putative enzymes of the SUMOylation pathway in the parasite Giardia lamblia. Although we observed several SUMOylated proteins, only the enzyme Arginine Deiminase (ADI) was confirmed as a SUMOylated substrate. ADI is involved in the survival of the parasite and, besides its role in ATP production, it also catalyzes the modification of arginine residues to citrulline in the cytoplasmic tail of surface proteins. During encystation, however, ADI translocates to the nuclei and downregulates the expression of the Cyst Wall Protein 2 (CWP2