Breugelmans, Bert;
Ansell, Brendan R. E.;
Young, Neil D.;
Amani, Parisa;
Stroehlein, Andreas J.;
Sternberg, Paul W.;
Jex, Aaron R.;
Boag, Peter R.;
Hofmann, Andreas;
Gasser, Robin B.
Flatworms have lost the right open reading frame kinase 3 gene during evolution
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Medientyp:
E-Artikel
Titel:
Flatworms have lost the right open reading frame kinase 3 gene during evolution
Beteiligte:
Breugelmans, Bert;
Ansell, Brendan R. E.;
Young, Neil D.;
Amani, Parisa;
Stroehlein, Andreas J.;
Sternberg, Paul W.;
Jex, Aaron R.;
Boag, Peter R.;
Hofmann, Andreas;
Gasser, Robin B.
Erschienen:
Springer Science and Business Media LLC, 2015
Beschreibung:
<jats:title>Abstract</jats:title><jats:p>All multicellular organisms studied to date have three <jats:italic><jats:underline>ri</jats:underline></jats:italic>ght <jats:italic><jats:underline>o</jats:underline></jats:italic>pen reading frame kinase genes (designated <jats:italic>riok-1</jats:italic>, <jats:italic>riok-2</jats:italic> and <jats:italic>riok-3</jats:italic>). Current evidence indicates that <jats:italic>riok-1</jats:italic> and <jats:italic>riok-2</jats:italic> have essential roles in ribosome biosynthesis and that the <jats:italic>riok-3</jats:italic> gene assists this process. In the present study, we conducted a detailed bioinformatic analysis of the <jats:italic>riok</jats:italic> gene family in 25 parasitic flatworms (platyhelminths) for which extensive genomic and transcriptomic data sets are available. We found that none of the flatworms studied have a <jats:italic>riok-3</jats:italic> gene, which is unprecedented for multicellular organisms. We propose that, unlike in other eukaryotes, the loss of RIOK-3 from flatworms does not result in an evolutionary disadvantage due to the unique biology and physiology of this phylum. We show that the loss of RIOK-3 coincides with a loss of particular proteins associated with essential cellular pathways linked to cell growth and apoptosis. These findings indicate multiple, key regulatory functions of RIOK-3 in other metazoan species. Taking advantage of a known partial crystal structure of human RIOK-1, molecular modelling revealed variability in nucleotide binding sites between flatworm and human RIOK proteins.</jats:p>