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Title: Cyanophage MazG is a pyrophosphohydrolase but unable to hydrolyse magic spot nucleotides.
Authors: Rihtman, B
Bowman-Grahl, S
Millard, A
Corrigan, RM
Clokie, MRJ
Scanlan, DJ
First Published: 27-Feb-2019
Publisher: Wiley, Society for Applied Microbiology (SfAM)
Citation: Environmental Microbiology Reports, 2019, 11(3) pp. 448-455
Abstract: Bacteriophage 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.
DOI Link: 10.1111/1758-2229.12741
eISSN: 1758-2229
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 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.
Description: Additional Supporting Information may be found in the online version of this article at the publisher’s web-site.
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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