Macrodomain protein from Streptomyces coelicolor - SCO6735 reverses T-linked DNA ADP-ribosylation (CROSBI ID 700262)
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Podaci o odgovornosti
Hloušek-Kasun, Andrea ; Mikolčević, Petra ; Jankevicius, Gytis ; Tromans-Coia, Callum ; Sabljić, Igor ; Bertoša, Branimir ; Ahel, Ivan ; Mikoč, Andreja
engleski
Macrodomain protein from Streptomyces coelicolor - SCO6735 reverses T-linked DNA ADP-ribosylation
Diverse proteins that constitute ADP- ribosylation metabolic cycle have been found in bacteria from the genus Streptomyces. We focused on the macrodomain family of ADP- ribosyl hydrolases that encompass key players in the recognition, interpretation, and turnover of ADP-ribose signaling. In Streptomyces, ADP-ribosylation is involved in the regulation of morphological differentiation and antibiotic production. Our results on ADP- ribosyl hydrolase from S. coelicolor - SCO6735 showed that disruption of SCO6735 increases production of antibiotic actinorhodin. We structurally and biochemically characterized SCO6735 protein. The crystal structure of SCO6735 revealed highly conserved three- layered α-β-α sandwich macrodomain fold with a deep cleft that represents a putative ligand- binding site. Currently, we are employing different molecular modelling methods in order to pinpoint catalytic mechanism of SCO6735 protein. Experiments in vitro showed that SCO6735 is active on both protein and DNA modified substrates ; it efficiently reverses protein ADP-ribosylation on glutamate residues and DNA ADP-ribosylation on thymidines that have been modified by DarT toxin. SCO6735 activity in vivo has been shown in E. coli ; when SCO6735 and DarT are co-expressed, SCO6735 can rescue E. coli from the toxic effect of DarT.
ADP-ribosylation, ADP-ribosyl hydrolase, DNA ADP-ribosylation, Macrodomain, Streptomyces coelicolor
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Podaci o prilogu
28
2019.
objavljeno
Podaci o matičnoj publikaciji
PARP 2019
Curtin, Nikola ; Corda, Daniela ; Yelamos, Jose ; Bai, Peter
Budimpešta:
Podaci o skupu
PARP 2019
poster
20.05.2019-23.05.2019
Budimpešta, Mađarska