ArticlePloS one2012
The two PPX-GppA homologues from Mycobacterium tuberculosis have distinct biochemical activities.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Article
- Biomolecular condensates as stress sensors and modulators of bacterial signaling.PLoS pathogens · 2024Review
- Mycobacterial Biofilm: Mechanisms, Clinical Problems, and Treatments.International journal of molecular sciences · 2024Review
- Ppx1 putative exopolyphosphatase is essential for polyphosphate accumulation inApplied and environmental microbiology · 2024Article
- Polyphosphate kinase-1 regulates bacterial and host metabolic pathways involved in pathogenesis ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functional Characterization of Small Alarmone Synthetase and Small Alarmone Hydrolase Proteins from Treponema denticola.Microbiology spectrum · 2023Article
- Targeting theFrontiers in microbiology · 2021Review
- Polyphosphate is an extracellular signal that can facilitate bacterial survival in eukaryotic cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The (p)ppGpp Synthetase RSH Mediates Stationary-Phase Onset and Antibiotic Stress Survival in Clostridioides difficile.Journal of bacteriology · 2020Article
- Functional Insights Into the Role ofFrontiers in microbiology · 2020Article
- Tolerance and Persistence to Drugs: A Main Challenge in the Fight AgainstFrontiers in microbiology · 2020Review
- Inorganic polyphosphate accumulation suppresses the dormancy response and virulence inThe Journal of biological chemistry · 2019Article
- Inhibiting the stringent response blocksScience advances · 2019Article
- Article
- The stringent response and Mycobacterium tuberculosis pathogenesis.Pathogens and disease · 2018Review
- Distribution Patterns of Polyphosphate Metabolism Pathway and Its Relationships With Bacterial Durability and Virulence.Frontiers in microbiology · 2018Article
- Phylogenetic analysis of proteins involved in the stringent response in plant cells.Journal of plant research · 2017Article
- Stringent Response Factors PPX1 and PPK2 Play an Important Role in Mycobacterium tuberculosis Metabolism, Biofilm Formation, and Sensitivity to Isoniazid In Vivo.Antimicrobial agents and chemotherapy · 2016Article
- Purification, crystallization and X-ray crystallographic analysis of a putative exopolyphosphatase from Zymomonas mobilis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis.Bioscience reports · 2015Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inorganic polyphosphate (poly-P), guanosine pentaphosphate (pppGpp) and guanosine tetraphosphate (ppGpp) are ubiquitous in bacteria. These molecules play a variety of important physiological roles associated with stress resistance, persistence, and virulence. In the bacterial pathogen Mycobacterium tuberculosis, the identities of the proteins responsible for the metabolism of polyphosphate and (p)ppGpp remain to be fully established. M. tuberculosis encodes two PPX-GppA homologues, Rv0496 (MTB-PPX1) and Rv1026, which share significant sequence similarity with bacterial exopolyphosphatase (PPX) and guanosine pentaphosphate 5'-phosphohydrolase (GPP) proteins. Here we delineate the respective biochemical activities of the Rv0496 and Rv1026 proteins and benchmark these against the activities of the PPX and GPP proteins from Escherichia coli. We demonstrate that Rv0496 functions as an exopolyphosphatase, showing a distinct preference for relatively short-chain poly-P substrates. In contrast, Rv1026 has no detectable exopolyphosphatase activities. Analogous to the E. coli PPX and GPP enzymes, the exopolyphosphatase activities of Rv0496 are inhibited by pppGpp and, to a lesser extent, by ppGpp alarmones, which are produced during the bacterial stringent response. However, neither Rv0496 nor Rv1026 have the ability to hydrolyze pppGpp to ppGpp; a reaction catalyzed by E. coli PPX and GPP. Both the Rv0496 and Rv1026 proteins have modest ATPase and to a lesser extent ADPase activities. pppGpp alarmones inhibit the ATPase activities of Rv1026 and, to a lesser extent, the ATPase activities of Rv0496. We conclude that PPX-GppA family proteins may not possess all the catalytic activities implied by their name and may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways.
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