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dc.contributor.authorRihtman, B-
dc.contributor.authorBowman-Grahl, S-
dc.contributor.authorMillard, A-
dc.contributor.authorCorrigan, RM-
dc.contributor.authorClokie, MRJ-
dc.contributor.authorScanlan, DJ-
dc.identifier.citationEnvironmental Microbiology Reports, 2019, 11(3) pp. 448-455en
dc.descriptionAdditional Supporting Information may be found in the online version of this article at the publisher’s web-site.en
dc.description.abstractBacteriophage possess a variety of auxiliary metabolic genes (AMGs) of bacterial origin. These proteins enable them to maximise infection efficiency, subverting bacterial metabolic processes for the purpose of viral genome replication and synthesis of the next generation of virion progeny. Here, we examined the enzymatic activity of a cyanophage MazG protein - a putative pyrophosphohydrolase previously implicated in regulation of the stringent response via reducing levels of the central alarmone molecule (p)ppGpp. We demonstrate however, that the purified viral MazG shows no binding or hydrolysis activity against (p)ppGpp. Instead, dGTP and dCTP appear to be the preferred substrates of this protein, consistent with a role preferentially hydrolysing deoxyribonucleotides from the high GC content host Synechococcus genome. This showcases a new example of the fine-tuned nature of viral metabolic processes.en
dc.description.sponsorshipB. R. was in receipt of a Chancellor's International PhD Scholarship from the University of Warwick. R.M.C. was supported by funding from the Wellcome Trust and Royal Society grant 104110. This work was also supported by the Natural Environment Research Council through Research Grants NE/J02273X/1 and NE/N003241/1. Bioinformatics analysis was carried out using MRC CLIMB Infrastructure (grant MR/L015080/1).en
dc.publisherWiley, Society for Applied Microbiology (SfAM)en
dc.rightsCopyright © the authors, 2019. This is an open-access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.titleCyanophage MazG is a pyrophosphohydrolase but unable to hydrolyse magic spot nucleotides.en
dc.typeJournal Articleen
dc.description.versionPublisher Versionen
dc.type.subtypeJournal Article-
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCESen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/School of Medicineen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/School of Medicine/Department of Infection, Immunity and Inflammationen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/Themesen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/Themes/Genome Scienceen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/Themes/Microbial Scienceen
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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