DISTRIBUTION OF PROTEIN POLY(ADP‐RIBOSYL)ATION SYSTEMS ACROSS ALL DOMAINS OF LIFE

Autor: Perina, Dragutin, Mikoč, Andreja, Ahel, Josip, Ćetković, Helena, Žaja, Roko, Ahel, Ivan
Přispěvatelé: Klobučar, Göran, Kopjar, Nevenka, Gligora Udovič, Marija, Lukša, Žaklin, Jelić, Dušan
Jazyk: angličtina
Rok vydání: 2015
Předmět:
Popis: Poly(ADP‐ribosyl)ation is a post‐translational modification of proteins involved in regulation of many cellular pathways. Poly(ADP‐ribose) (PAR) consists of chains of repeating ADP‐ribose nucleotide units and is synthesized by the family of enzymes called poly(ADP‐ribose) polymerases (PARPs). This modification can be removed by the hydrolytic action of poly(ADP‐ribose) glycohydrolase (PARG) and ADP‐ribosylhydrolase 3 (ARH3). Hydrolytic activity of macrodomain proteins (MacroD1, MacroD2 and TARG1) is responsible for the removal of terminal ADP‐ribose unit and for complete reversion of protein ADP‐ribosylation. Poly(ADP‐ribosyl)ation is widely utilized in eukaryotes and PARPs are present in representatives from all six major eukaryotic supergroups, with only a small number of eukaryotic species that do not possess PARP genes. The last common ancestor of all eukaryotes possessed at least five types of PARP proteins that include both mono and poly(ADP‐ribosyl) transferases. Distribution of PARGs strictly follows the distribution of PARP proteins in eukaryotic species. At least one of the macrodomain proteins that hydrolyse terminal ADP‐ribose is also always present. Therefore, we can presume that the last common ancestor of all eukaryotes possessed a fully functional and reversible PAR metabolism and that PAR signalling provided the conditions essential for survival of the ancestral eukaryote in its ancient environment.
Databáze: OpenAIRE