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http://purl.uniprot.org/citations/20529853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20529853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20529853http://www.w3.org/2000/01/rdf-schema#comment"MazG nucleoside triphosphate pyrophosphohydrolase (NTP-PPase, EC 3.6.1.8) from the avirulent Mycobacterium tuberculosis H37Ra contains a spontaneous mutation on a highly conserved residue, resulting in an A219E substitution (MtMazG[A219E]). In this work, we show that mycobacterial MazG from either the virulent M. tuberculosis H37Rv (MtMazG) or the fast-growing Mycobacterium smegmatis (MsMazG) is a potent NTP-PPase capable of hydrolyzing all canonical (d)NTPs, as well as the mutagenic dUTP and 8-oxo-7,8-dihydro-2'-dGTP. However, this hydrolysis activity is diminished by the MtMazG[A219E] mutation. Moreover, deletion of mazG in M. smegmatis rendered the mycobacteria defective in response to oxidative stress. Importantly, expression of the wild-type MtMazG, but not the A219E mutant, restored cell viability under oxidative stress. Intriguingly, under oxidative stress, both the mazG-null and MtMazG[A219E]-expressing M. smegmatis strains failed to elevate relA, while retaining their ability to up-regulate sigE, suggesting a specific role for the MazG NTP-PPase activity in oxidative stress-triggered, transcriptional activation of relA. The MtMazG is a homotetramer with each subunit containing a single MazG core domain flanked by two regions, both of which are essential for NTP-PPase activity. Taken together, these results demonstrate that the mycobacterial MazG is a potent NTP-PPase and that this activity is required to maintain the full capacity of the mycobacteria to respond to oxidative stress. Our work implicates a role for the MazG activity in the virulence of M. tuberculosis."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.088872"xsd:string
http://purl.uniprot.org/citations/20529853http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.088872"xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Sun Q."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Sun Q."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Zhong Y."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Zhong Y."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Zhao G.P."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Zhao G.P."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Fan X.Y."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Fan X.Y."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Yao Y.F."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Yao Y.F."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Lu L.D."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/author"Lu L.D."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/pages"28076-28085"xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/pages"28076-28085"xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/title"Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response."xsd:string
http://purl.uniprot.org/citations/20529853http://purl.uniprot.org/core/title"Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response."xsd:string