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

Authors
  • Schrumpfová, Petra Procházková1, 2
  • Vychodilová, Ivona1, 2
  • Hapala, Jan1, 2
  • Schořová, Šárka1, 2
  • Dvořáček, Vojtěch1, 3
  • Fajkus, Jiří4, 5, 6
  • 1 Mendel Centre for Plant Genomics and Proteomics, CEITEC - Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic. , (Czechia)
  • 2 Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic. , (Czechia)
  • 3 Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Královopolská 135, 61265, Brno, Czech Republic. , (Czechia)
  • 4 Mendel Centre for Plant Genomics and Proteomics, CEITEC - Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic. [email protected] , (Czechia)
  • 5 Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic. [email protected] , (Czechia)
  • 6 Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Královopolská 135, 61265, Brno, Czech Republic. [email protected] , (Czechia)
Type
Published Article
Journal
Plant molecular biology
Publication Date
Jan 01, 2016
Volume
90
Issue
1-2
Pages
189–206
Identifiers
DOI: 10.1007/s11103-015-0409-8
PMID: 26597966
Source
Medline
Keywords
License
Unknown

Abstract

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.

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