lnu.sePublikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Non-host class II ribonucleotide reductase in Thermus viruses: sequence adaptation and host interaction
Tech Univ Dresden, Germany.
Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för biologi och miljö (BOM). (Ctr Ecol & Evolut Microbial Model Syst EEMiS)ORCID-id: 0000-0002-6887-6661
Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för biologi och miljö (BOM). Stockholm University, Sweden. (Ctr Ecol & Evolut Microbial Model Syst EEMiS)ORCID-id: 0000-0002-8779-6464
2019 (Engelska)Ingår i: PeerJ, ISSN 2167-8359, E-ISSN 2167-8359, Vol. 7, s. 1-17, artikel-id e6700Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Ribonucleotide reductases (RNR) are essential enzymes for all known life forms. Their current taxonomic distribution suggests extensive horizontal gene transfer e.g., by processes involving viruses. To improve our understanding of the underlying processes, we characterized a monomeric class II RNR (NrdJm) enzyme from a Thermus virus, a subclass not present in any sequenced Thermus spp. genome. Phylogenetic analysis revealed a distant origin of the nrdJm gene with the most closely related sequences found in mesophiles or moderate thermophiles from the Firmicutes phylum. GC-content, codon usage and the ratio of coding to non-coding substitutions (dN/dS) suggest extensive adaptation of the gene in the virus in terms of nucleotide composition and amino acid sequence. The NrdJm enzyme is a monomeric B-12-dependent RNR with nucleoside triphosphate specificity. It exhibits a temperature optimum at 60-70 degrees C, which is in the range of the growth optimum of Thermus spp. Experiments in combination with the Thermus thermophilus thioredoxin system show that the enzyme is able to retrieve electrons from the host NADPH pool via host thioredoxin and thioredoxin reductases. This is different from other characterized viral RNRs such as T4 phage RNR, where a viral thioredoxin is present. We hence show that the monomeric class II RNR, present in Thermus viruses, was likely transferred from an organism phylogenetically distant from the one they were isolated from, and adapted to the new host in genetic signature and amino acids sequence.

Ort, förlag, år, upplaga, sidor
PeerJ Incorporation , 2019. Vol. 7, s. 1-17, artikel-id e6700
Nyckelord [en]
Ribonucleotide reductase, Horizontal gene transfer, Bacteriophage-derived enzymes, Thioredoxin, Transduction, Host-adaptation
Nationell ämneskategori
Mikrobiologi
Forskningsämne
Biomedicinsk vetenskap, Virologi
Identifikatorer
URN: urn:nbn:se:lnu:diva-82037DOI: 10.7717/peerj.6700ISI: 000463695300002OAI: oai:DiVA.org:lnu-82037DiVA, id: diva2:1306433
Tillgänglig från: 2019-04-23 Skapad: 2019-04-23 Senast uppdaterad: 2019-04-23Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltext

Personposter BETA

Holmfeldt, KarinLundin, Daniel

Sök vidare i DiVA

Av författaren/redaktören
Holmfeldt, KarinLundin, Daniel
Av organisationen
Institutionen för biologi och miljö (BOM)
I samma tidskrift
PeerJ
Mikrobiologi

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetricpoäng

doi
urn-nbn
Totalt: 25 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf