Cyanophage MazG is a pyrophosphohydrolase but unable to hydrolyse magic spot nucleotides
| Autor: | Rebecca M. Corrigan, Martha R. J. Clokie, Andrew D. Millard, Sabine Bowman‐Grahl, Branko Rihtman, David J. Scanlan |
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| Rok vydání: | 2019 |
| Předmět: |
Stringent response
viruses Deoxyribonucleotides Substrate Specificity Bacterial genetics Bacteriophage Viral Proteins 03 medical and health sciences Bacterial Proteins Catalytic Domain Bacteriophages Amino Acid Sequence Pyrophosphatases Gene Phylogeny Ecology Evolution Behavior and Systematics 030304 developmental biology QR355 Synechococcus chemistry.chemical_classification Base Composition 0303 health sciences biology 030306 microbiology Brief Report Hydrolysis Cyanophage biology.organism_classification Agricultural and Biological Sciences (miscellaneous) Recombinant Proteins Enzyme Biochemistry chemistry Brief Reports Viral genome replication Genome Bacterial Alarmone |
| Zdroj: | Environmental Microbiology Reports |
| ISSN: | 1758-2229 |
| DOI: | 10.1111/1758-2229.12741 |
| Popis: | 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.\ud |
| Databáze: | OpenAIRE |
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