Cited by 358Telomeres, Telomerase, and SenescenceGenomics and Chromatin DynamicsDNA and Nucleic Acid Chemistry

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TRF1 is a dimer and bends telomeric DNA

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Bianchi, Alessandro, Smith, Susan, Chong, Laura, Elias, Peter, de Lange, Titia·1997·The EMBO Journal

DOI 10.1093/emboj/16.7.1785PMC PMC1169781

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Abstract

TRF1 is a mammalian telomeric protein that binds to the duplex array of TTAGGG repeats at chromosome ends. TRF1 has homology to the DNA-binding domain of the Myb family of transcription factors but, unlike most Myb-related proteins, TRF1 carries one rather than multiple Myb-type DNA-binding motifs. Here we show that TRF1 binds DNA as a dimer using a large conserved domain near the N-terminus of the protein for TRF1-TRF1 interactions. Dimerization was observed both in a complex with DNA and in the yeast two-hybrid assay. TRF1 dimers were found to require both Myb repeats for the formation of a stable complex with DNA, indicating a parallel between the DNA-binding mode of TRF1 and other Myb-related proteins. TRF1 was found to have a number of biochemical similarities to Rap1p, a distantly related DNA-binding protein that functions at telomeres in yeast. Rap1p and TRF1 both require two Myb motifs for DNA binding and both factors bind along their cognate telomeric sequences without showing strong cooperative interactions between adjacent proteins. Furthermore, TRF1 was found to bend its telomeric site to an angle of -120 degrees. Since Rap1p similarly distorts telomeric DNA, we propose that DNA bending is important for the function of telomeres in yeast and mammals.

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Authors: Bianchi, A., Smith, S., Chong, L., Elias, P., & de Lange, T.
Affiliations: Rockefeller University (US)
ORCID: Bianchi, Alessandro
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1997-04-01
Volume: 16
Issue: 7
Pages: 1785-1794
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/16.7.1785
PMC: PMC1169781
OpenAlex: W2127440297
Cited by: 358
References: 67
Citations by year: 2026: 5 · 2025: 4 · 2024: 11 · 2023: 10 · 2022: 6 · 2021: 16 · 2020: 3 · 2019: 13 · 2018: 5 · 2017: 14 · 2016: 8 · 2015: 9 · 2014: 17 · 2013: 12 · 2012: 13
FWCI: 8.57
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
University of North Carolina at Chapel Hill
Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords: TRF1, telomeres, protein dimerization, DNA bending, TTAGGG repeats, Rap1p, telomeric DNA binding, telomere function, protein-DNA complex
MeSH terms: Shelterin Complex, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, DNA, DNA-Binding Proteins, Mammals, Nucleic Acid Conformation, Recombinant Proteins, Repetitive Sequences, Nucleic Acid, Saccharomyces cerevisiae, Transcription Factors, Transcription, Genetic, Transfection, Protein Biosynthesis, Polymerase Chain Reaction, Telomere, Conserved Sequence, Spodoptera, Dimerization, Saccharomyces cerevisiae Proteins, Telomere-Binding Proteins, Telomeric Repeat Binding Protein 1, Macromolecular Substances

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TRF1 is a dimer and bends telomeric DNA

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