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Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase (CROSBI ID 188387)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Dunstan, Mark S. ; Barkauskaite, Eva ; Lafite, Pierre ; Knežević, Claire E. ; Brassington, Amy ; Ahel, Marijan ; Hergenrother, Paul J. ; Leys, David ; Ahel, Ivan Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase // Nature communications, 3 (2012), 6; Article Number 8-x. doi: 10.1038/ncomms1889

Podaci o odgovornosti

Dunstan, Mark S. ; Barkauskaite, Eva ; Lafite, Pierre ; Knežević, Claire E. ; Brassington, Amy ; Ahel, Marijan ; Hergenrother, Paul J. ; Leys, David ; Ahel, Ivan

engleski

Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase

Poly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of a number of cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the unique PAR (1 ''-2') ribose-ribose bonds. Here we report the structure and mechanism of the first canonical PARG from the protozoan Tetrahymena thermophila. In addition, we reveal the structure of T. thermophila PARG in a complex with a novel rhodanine-containing mammalian PARG inhibitor RBPI-3. Our data demonstrate that the protozoan PARG represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors.

identification; chromatin; inhibition; activation; proteins; model; field; PARG

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Podaci o izdanju

3 (6)

2012.

Article Number 8-x

objavljeno

2041-1723

10.1038/ncomms1889

Povezanost rada

Geologija

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