Telomere binding protein TRB1 is associated with promoters of translation machinery genes in vivo

Telomere binding protein TRB1 is associated with promoters of translation machinery genes in vivo Recently we characterised TRB1, a protein from a single-myb-histone family, as a structural and functional component of telomeres in Arabidopsis thaliana. TRB proteins, besides their ability to bind specifically to telomeric DNA using their N-terminally positioned myb-like domain of the same type as in human shelterin proteins TRF1 or TRF2, also possess a histone-like domain which is involved in protein–protein interactions e.g., with POT1b. Here we set out to investigate the genome-wide localization pattern of TRB1 to reveal its preferential sites of binding to chromatin in vivo and its potential functional roles in the genome-wide context. Our results demonstrate that TRB1 is preferentially associated with promoter regions of genes involved in ribosome biogenesis, in addition to its roles at telomeres. This preference coincides with the frequent occurrence of telobox motifs in the upstream regions of genes in this category, but it is not restricted to the presence of a telobox. We conclude that TRB1 shows a specific genome-wide distribution pattern which suggests its role in regulation of genes involved in biogenesis of the translational machinery, in addition to its preferential telomeric localization. Plant Molecular Biology Springer Journals

Telomere binding protein TRB1 is associated with promoters of translation machinery genes in vivo

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Springer Netherlands
Copyright © 2015 by Springer Science+Business Media Dordrecht
Life Sciences; Plant Sciences; Biochemistry, general; Plant Pathology
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  • AtTRB1, a telomeric DNA-binding protein from Arabidopsis, is concentrated in the nucleolus and shows highly dynamic association with chromatin
    Dvorackova, M; Rossignol, P; Shaw, PJ; Koroleva, OA; Doonan, JH; Fajkus, J
  • Chromatin dynamics of plant telomeres and ribosomal genes
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  • Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities
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  • POT1-TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation
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  • Extending the model of Arabidopsis telomere length and composition across Brassicaceae
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