Nudix proteins affecting microbial pathogenesis

Kraszewska, Elzbieta; Drabinska, Joanna

doi:10.1099/mic.0.000993

Cited by 3 publications

(2 citation statements)

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“…We close with an interesting review on Nudix proteins and their role in bacterial pathogenesis from Elzbieta Kraszewska and Joanna Drabinska at the Polish Academy of Science in Warsaw, Poland [18]. These proteins, exemplified by E.…”

Section: Full-textmentioning

confidence: 99%

Microbial Musings – December 2020

Thomas

2020

Microbiology

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Section: Full-textmentioning

confidence: 99%

Microbial Musings – December 2020

Thomas

2020

Microbiology

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“…To avoid the detrimental effects of 8-oxoG, organisms are equipped with mechanisms that eliminate oxidized RNA ( 15 – 17 ). As an example, the MutT protein in Escherichia coli and its mammalian homologs (such as MutT homolog 1 [MTH1]) cleave ribonucleotides carrying 8-oxoG by hydrolyzing the oxidized nucleoside diphosphates and/or triphosphates to monophosphates ( 18 , 19 ), preventing the incorporation of the free oxidized nucleotides into RNA synthesis. Although the oxidized forms of RNA precursor nucleotides can be efficiently removed in such manner, 8-oxoG can also be formed in the RNA molecules already present within the cell by direct oxidation of the base ( 20 ).…”

Section: Introductionmentioning

confidence: 99%

PNPase and RhlB Interact and Reduce the Cellular Availability of Oxidized RNA in Deinococcus radiodurans

et al. 2022

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Oxidative RNA damage can be caused by oxidative stress, such as hydrogen peroxide, ionizing radiation, and antibiotic treatment. 8-oxo-7,8-dihydroguanine (8-oxoG), a major type of oxidized RNA, is highly mutagenic and participates in a variety of disease occurrences and development. Although several proteins have been identified to recognize 8-oxoG-modified RNA, the knowledge of how RNA oxidative damage is controlled largely remains unclear, especially in nonmodel organisms.

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Coagulase-negative staphylococci release a purine analog that inhibits Staphylococcus aureus virulence

et al. 2021

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Coagulase-negative staphylococci and Staphylococcus aureus colonize similar niches in mammals and conceivably compete for space and nutrients. Here, we report that a coagulase-negative staphylococcus, Staphylococcus chromogenes ATCC43764, synthesizes and secretes 6-thioguanine (6-TG), a purine analog that suppresses S. aureus growth by inhibiting de novo purine biosynthesis. We identify a 6-TG biosynthetic gene cluster in S. chromogenes and other coagulase-negative staphylococci including S. epidermidis, S. pseudintermedius and S. capitis. Recombinant S. aureus strains harbouring this operon produce 6-TG and, when used in subcutaneous co-infections in mice with virulent S. aureus USA300, protect the host from necrotic lesion formation. Used prophylactically, 6-TG reduces necrotic skin lesions in mice infected with USA300, and this effect is mediated by abrogation of toxin production. RNAseq analyses reveal that 6-TG downregulates expression of genes coding for purine biosynthesis, the accessory gene regulator (agr) and ribosomal proteins in S. aureus, providing an explanation for its effect on toxin production.

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Nudix proteins affecting microbial pathogenesis

Cited by 3 publications

References 50 publications

Microbial Musings – December 2020

Microbial Musings – December 2020

PNPase and RhlB Interact and Reduce the Cellular Availability of Oxidized RNA in Deinococcus radiodurans

Coagulase-negative staphylococci release a purine analog that inhibits Staphylococcus aureus virulence

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