Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Telomere Binding Protein TRB1 Preferentially Associates with Promoters of Translation Machinery genes


ABSTRACT: Background: 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 telomeric DNA using their N-terminally positioned myb-like domain of the same type as in human TRF1 or TRF2 shelterin proteins, possess also histone-like domain which is involved in protein-protein interactions e.g., with POT1b. We set to investigate the genome-wide localization pattern of TRB1 to reveal its preferential mode of binding to chromatin in vivo and its potential functional roles in the genome-wide context. Results: Our results demonstrate that in addition to its roles at telomeres, TRB1 is preferentially associated with promoter regions of genes involved in ribosome biogenesis. This preference coincides with a frequent occurrence of telobox motifs in the upstream regions of genes in this category, but is not restricted to the telobox presence. Conclusions: We conclude that TRB1, in addition to its preferential telomeric localization, shows a specific genome-wide distribution pattern suggesting its role in regulation of genes involved in biogenesis of translational machinery. TRB1 DNA-binding activity investigated in 2 biological replicates (2 immunoprecipitation approaches) with controls; with technical replicates.

ORGANISM(S): Arabidopsis thaliana

SUBMITTER: Jan Hapala 

PROVIDER: E-GEOD-69431 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

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

Schrumpfová Petra Procházková PP   Vychodilová Ivona I   Hapala Jan J   Schořová Šárka Š   Dvořáček Vojtěch V   Fajkus Jiří J  

Plant molecular biology 20151123 1-2


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 localiz  ...[more]

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