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dc.contributor.authorNasaev, Shamsudin S.
dc.contributor.authorKopeykina, Anna S.
dc.contributor.authorKuznetsova, Ksenia
dc.contributor.authorLevitsky, Lev I.
dc.contributor.authorMoshkovskii, Sergei A.
dc.date.accessioned2022-12-19T14:04:17Z
dc.date.available2022-12-19T14:04:17Z
dc.date.created2022-12-06T14:26:20Z
dc.date.issued2022
dc.identifier.issn0006-2979
dc.identifier.urihttps://hdl.handle.net/11250/3038614
dc.description.abstractRNA editing by adenosine deaminases of the ADAR family can lead to protein recoding, since inosine formed from adenosine in mRNA is complementary to cytosine; the resulting codon editing might introduce amino acid substitutions into translated proteins. Proteome recoding can have functional consequences which have been described in many animals including humans. Using protein recoding database derived from publicly available transcriptome data, we identified for the first time the recoding sites in the zebrafish shotgun proteomes. Out of more than a hundred predicted recoding events, ten substitutions were found in six used datasets. Seven of them were in the AMPA glutamate receptor subunits, whose recoding has been well described, and are conserved among vertebrates. Three sites were specific for zebrafish proteins and were found in the transmembrane receptors astrotactin 1 and neuregulin 3b (proteins involved in the neuronal adhesion and signaling) and in the rims2b gene product (presynaptic membrane protein participating in the neurotransmitter release), respectively. Further studies are needed to elucidate the role of recoding of the said three proteins in the zebrafish.en_US
dc.language.isoengen_US
dc.publisherSpringeren_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleProteomic Analysis of Zebrafish Protein Recoding via mRNA Editing by ADAR Enzymesen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2022 The Author(s)en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1
dc.identifier.doi10.1134/S0006297922110098
dc.identifier.cristin2089498
dc.source.journalBiochemistry (Moscow)en_US
dc.source.pagenumber1301-1309en_US
dc.identifier.citationBiochemistry (Moscow). 2022, 87 (11), 1301-1309.en_US
dc.source.volume87en_US
dc.source.issue11en_US


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