Hide metadata

dc.date.accessioned2017-08-09T10:12:33Z
dc.date.available2017-08-09T10:12:33Z
dc.date.created2012-07-25T14:19:10Z
dc.date.issued2012
dc.identifier.citationSandvik, Guro Katrine Tomter, Ane Berg Bergan, Jonas Zoppellaro, Giorgio Barra, Anne-Laure Røhr, Åsmund Kjendseth Kolberg, Matthias Ellefsen, Stian Andersson, K. Kristoffer Nilsson, Göran Erik . Studies of Ribonucleotide Reductase in Crucian Carp-An Oxygen Dependent Enzyme in an Anoxia Tolerant Vertebrate. PLoS ONE. 2012, 7(8)
dc.identifier.urihttp://hdl.handle.net/10852/56918
dc.description.abstractThe enzyme ribonucleotide reductase (RNR) catalyzes the conversion of ribonucleotides to deoxyribonucleotides, the precursors for DNA. RNR requires a thiyl radical to activate the substrate. In RNR of eukaryotes (class Ia RNR), this radical originates from a tyrosyl radical formed in reaction with oxygen (O2) and a ferrous di-iron center in RNR. The crucian carp (Carassius carassius) is one of very few vertebrates that can tolerate several months completely without oxygen (anoxia), a trait that enables this fish to survive under the ice in small ponds that become anoxic during the winter. Previous studies have found indications of cell division in this fish after 7 days of anoxia. This appears nearly impossible, as DNA synthesis requires the production of new deoxyribonucleotides and therefore active RNR. We have here characterized RNR in crucian carp, to search for adaptations to anoxia. We report the full-length sequences of two paralogs of each of the RNR subunits (R1i, R1ii, R2i, R2ii, p53R2i and p53R2ii), obtained by cloning and sequencing. The mRNA levels of these subunits were measured with quantitative PCR and were generally well maintained in hypoxia and anoxia in heart and brain. We also report maintained or increased mRNA levels of the cell division markers proliferating cell nuclear antigen (PCNA), brain derived neurotrophic factor (BDNF) and Ki67 in anoxic hearts and brains. Electron paramagnetic resonance (EPR) measurements on in vitro expressed crucian carp R2 and p53R2 proteins gave spectra similar to mammalian RNRs, including previously unpublished human and mouse p53R2 EPR spectra. However, the radicals in crucian carp RNR small subunits, especially in the p53R2ii subunit, were very stable at 0 °C. A long half-life of the tyrosyl radical during wintertime anoxia could allow for continued cell division in crucian carp.
dc.languageEN
dc.publisherPublic Library of Science (PLoS)
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleStudies of Ribonucleotide Reductase in Crucian Carp-An Oxygen Dependent Enzyme in an Anoxia Tolerant Vertebrate
dc.typeJournal article
dc.creator.authorSandvik, Guro Katrine
dc.creator.authorTomter, Ane Berg
dc.creator.authorBergan, Jonas
dc.creator.authorZoppellaro, Giorgio
dc.creator.authorBarra, Anne-Laure
dc.creator.authorRøhr, Åsmund Kjendseth
dc.creator.authorKolberg, Matthias
dc.creator.authorEllefsen, Stian
dc.creator.authorAndersson, K. Kristoffer
dc.creator.authorNilsson, Göran Erik
cristin.unitcode185,15,20,0
cristin.unitnameInstitutt for biovitenskap (tidl. IMBV)
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1
dc.identifier.cristin936061
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=PLoS ONE&rft.volume=7&rft.spage=&rft.date=2012
dc.identifier.jtitlePLoS ONE
dc.identifier.volume7
dc.identifier.issue8
dc.identifier.pagecount13
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0042784
dc.identifier.urnURN:NBN:no-59562
dc.type.documentTidsskriftartikkel
dc.type.peerreviewedPeer reviewed
dc.source.issn1932-6203
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/56918/2/journal.pone.0042784.pdf
dc.type.versionPublishedVersion
cristin.articleide42784


Files in this item

Appears in the following Collection

Hide metadata

Attribution 4.0 International
This item's license is: Attribution 4.0 International