Naslov
Bacterial PARP/PARG enzymes – filogenetic and structural comparisson

Autori
Mikolčević, Petra ; Hloušek-Kasun Andrea ; Andreja Mikoč

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
PARP2021 / - Barcelona, 2021, 23-23

Skup
PARP2021: Research on the Family of Poly(ADP-ribose) Polymerases

Mjesto i datum
Barcelona, Španjolska, 07.09.2021. - 10.09.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
ADP-ribozilacija, makrodomena, ADP-ribozilacija nukleinskih kiselina
(ADP-ribosylation, macrodomain, nucleic acid ADP-ribosylation)

Sažetak
ADP-ribosylation is an evolutionarily conserved reversible post-translational modification utilized from bacteria to humans. Bacteria were historically considered to be devoid of PAR metabolism, despite the fact many harbour genes homologous to the eukaryotic PARPs and PARGs. Here, we give a comprehensive overview and comparisson of bacterial PARP and PARG enzymes, their philogenetic analysis and architecture. Bacterial PARPs consist of (at most) three distinct domains – the N-terminal tryptophan- glycine-arginine (WGR) domain which is important for DNA-dependent activation, the mid-portion with an α-helix allosteric regulation domain (PARP_reg), followed by the ART domain (PARP) with the conserved catalytic glutamate. The seventy-two sequences containing at least the PARP catalytic domain are found distributed in six bacterial phyla (Actinobacteria, Bacteriodetes, Choloflexi, Cyanobacteria, Firmicutes, and Proteobacteria). Many bacterial species have a distant PARG homologue denoted as - DUF2263. Crystal structure of Thermomonospora curvata (TcPARG) DUF2263 has been resolved. Comparison with the available structures revealed an ADPr-binding macrodomain fold, the PARG signature sequence with previously identified key residues: two consecutive glutamates, and a novel type of N-terminal helical extension{; ; Slade, 2011 #468}; ; . The bacterial-type PARGs are believed to be confined only to act as exo-glycohydrolases. In several bacterial species - H. aurantiacus, C. difficile and Butyrivibrio proteoclasticus have the PARG and MacroD homologues forming a basic hydrolase duo, accompanying the PARPs – ensuring complete de- PARylation. Moreover, B. proteoclasticus and H. aurantiacus possess one and even more additional hydrolases, respectively. The presence of these comprehensive sets of proteins, which could perform a complete functional PAR metabolism indicate an adaptive advantage that has been preserved over time, rather than a simple horizontal gene transfer event as believed so far.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

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