Ribonucleotide reductases recapitulate biogeographic patterns within virioplankton according to ocean biogeochemistry

Abstract

Many of the important biogeochemical implications of marine viruses focus on the activity of lytic viruses. It is generally thought that lytic viral activity contributes to maintaining bioavailable nutrient pools and controlling host community composition through specific infection and lysis processes. Among lytic viruses, genome replication is under stringent selection pressure as advantages in replication speed and fidelity can influence viral fitness. Deoxyribonucleotides (dNTPs) are the precursor substrate for DNA synthesis and ribonucleotide reductase (RNR) is the only known enzyme capable of reducing ribonucleotides into dNTPs. Thus, for a virus, encoding an RNR gene provides control over dNTP production. Overall, distributional patterns of the RNR-encoding virioplankton community mirrored that seen for total virioplankton throughout the global ocean. A majority of RNR-encoding virioplankton ([~]66%) carried the Class II enzyme and most of these carried the monomeric (NrdJm) gene. This was significant as NrdJm utilizes triphosphate ribonucleotides as opposed to the diphosphate ribonucleotides used by Class I and Class II dimeric RNRs. The distribution and frequency of Class I RNRs followed the concentration of required iron and manganese co-factors. Oceanic virioplankton encompassed a high diversity of Class I and II RNRs with the discovery of new phylogenetic clades not previously observed among viruses or within cellular life. Representing [~]10% of all virioplankton populations, RNR-encoding viral populations demonstrated surprising fidelity with the major biogeographical features defining oceanic ecosystems.