Identification and characterization of three telomere repeat-binding factors in rice

Mi Young Byun, Jong P. Hong, Woo Taek Kim

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Telomeres consist of nucleoprotein complexes that protect chromosome end structures. Here, we describe three OsTRBF genes, encoding telomere repeat-binding factors of the single Myb histone family in rice. The predicted proteins contain a Myb DNA-binding motif and a linker histone H1/H5 domain in the N-terminal and central regions, respectively. The OsTRBF transcripts were constitutively detected in rice plants grown under greenhouse conditions. Gel retardation assays showed that these OsTRBF proteins bind specifically to the plant double-stranded telomeric sequence, TTTAGGG, with markedly different binding affinities as judged by their respective dissociation constants. Yeast two-hybrid and in vitro pull-down assays indicated that both OsTRBF1 and OsTRBF2 interact with one another to form homo- and hetero-complexes, while OsTRBF3 appeared to act as a monomer. Our results suggest that OsTRBFs play combinatory roles in the function and structure of telomeres in rice.

Original languageEnglish
Pages (from-to)85-90
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume372
Issue number1
DOIs
Publication statusPublished - 2008 Jul 18

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Telomere-Binding Proteins
Histones
Assays
Telomere
Gene encoding
Nucleoproteins
Greenhouses
Chromosomes
Yeast
Chromosome Structures
Nucleotide Motifs
Proteins
Monomers
Gels
Electrophoretic Mobility Shift Assay
DNA
Yeasts
Genes
Oryza

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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Identification and characterization of three telomere repeat-binding factors in rice. / Byun, Mi Young; Hong, Jong P.; Kim, Woo Taek.

In: Biochemical and Biophysical Research Communications, Vol. 372, No. 1, 18.07.2008, p. 85-90.

Research output: Contribution to journalArticle

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AB - Telomeres consist of nucleoprotein complexes that protect chromosome end structures. Here, we describe three OsTRBF genes, encoding telomere repeat-binding factors of the single Myb histone family in rice. The predicted proteins contain a Myb DNA-binding motif and a linker histone H1/H5 domain in the N-terminal and central regions, respectively. The OsTRBF transcripts were constitutively detected in rice plants grown under greenhouse conditions. Gel retardation assays showed that these OsTRBF proteins bind specifically to the plant double-stranded telomeric sequence, TTTAGGG, with markedly different binding affinities as judged by their respective dissociation constants. Yeast two-hybrid and in vitro pull-down assays indicated that both OsTRBF1 and OsTRBF2 interact with one another to form homo- and hetero-complexes, while OsTRBF3 appeared to act as a monomer. Our results suggest that OsTRBFs play combinatory roles in the function and structure of telomeres in rice.

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