TY - JOUR
T1 - Staphylococcus aureus MazG hydrolyzes oxidized guanine nucleotides and contributes to oxidative stress resistance
AU - Nigo, Fuki
AU - Nakagawa, Ryosuke
AU - Hirai, Yuuki
AU - Imai, Lina
AU - Suzuki, Yutaka
AU - Furuta, Kazuyuki
AU - Kaito, Chikara
N1 - Funding Information:
This study was supported by JSPS Grants-in-Aid for Scientific Research (grants 22H02869 , 22K19435 , 19H03466 , 16H06279 (PAGS) , and 221S0002 ), the Takeda Science Foundation (CK), the Ichiro Kanehara Foundation (CK), and the Ryobi Teien Memory Foundation (CK).
Publisher Copyright:
© 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)
PY - 2023/6
Y1 - 2023/6
N2 - We previously reported that knockout of the mazG (SA1292) gene decreases Staphylococcus aureus killing activity against silkworms. S. aureus MazG (SaMazG) has a nucleotide pyrophosphatase domain conserved among MazG family proteins, but its biochemical characteristics are unknown. In the present study, we purified recombinant N-terminal His-tagged SaMazG protein and examined its biochemical activity. SaMazG hydrolyzed GTP, UTP, dGTP, and TTP into nucleoside monophosphates. Hydrolytic activity of SaMazG against ATP, CTP, dATP, and dCTP was low or not detected. SaMazG exhibited high hydrolytic activity against 8-oxo-GTP and 8-oxo-dGTP, oxidized guanine nucleotides, with a Vmax/Km ratio more than 15-fold that of GTP. Furthermore, the S. aureus mazG knockout mutant was sensitive to hydrogen peroxide compared with the parent strain. These results suggest that SaMazG is a nucleotide pyrophosphatase hydrolyzing oxidized guanine nucleotides that contributes to the oxidative stress resistance of S. aureus.
AB - We previously reported that knockout of the mazG (SA1292) gene decreases Staphylococcus aureus killing activity against silkworms. S. aureus MazG (SaMazG) has a nucleotide pyrophosphatase domain conserved among MazG family proteins, but its biochemical characteristics are unknown. In the present study, we purified recombinant N-terminal His-tagged SaMazG protein and examined its biochemical activity. SaMazG hydrolyzed GTP, UTP, dGTP, and TTP into nucleoside monophosphates. Hydrolytic activity of SaMazG against ATP, CTP, dATP, and dCTP was low or not detected. SaMazG exhibited high hydrolytic activity against 8-oxo-GTP and 8-oxo-dGTP, oxidized guanine nucleotides, with a Vmax/Km ratio more than 15-fold that of GTP. Furthermore, the S. aureus mazG knockout mutant was sensitive to hydrogen peroxide compared with the parent strain. These results suggest that SaMazG is a nucleotide pyrophosphatase hydrolyzing oxidized guanine nucleotides that contributes to the oxidative stress resistance of S. aureus.
KW - 8-Oxo-GTP
KW - MazG
KW - Nucleotide pyrophosphatase
KW - Oxidative stress
KW - Staphylococcus aureus
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U2 - 10.1016/j.biochi.2023.02.001
DO - 10.1016/j.biochi.2023.02.001
M3 - Article
C2 - 36746255
AN - SCOPUS:85148700624
SN - 0300-9084
VL - 209
SP - 52
EP - 60
JO - Biochimie
JF - Biochimie
ER -