The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
TRF1 is a dimer and bends telomeric DNA
Open accessAbstract
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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“TRF1 has the ability to induce bending, looping, and pairing of duplex telomeric DNA (5, 6, 20, 21), activities that could facilitate the folding back of the telomere.”
From Control of Human Telomere Length by TRF1 and TRF2 (2000) · cites this paper as [5]
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Cites
A novel genetic system to detect protein–protein interactions
Fields, S., & Song, O.-K. (1989) · Nature · doi:10.1038/340245a0 · Cited by 6,152
Moyzis, R. K., Buckingham, J. M., Cram, L. S., Dani, M. A. C., Deaven, L. L., Jones, M. D., Meyne, J., Ratliff, R. L., & Wu, J. R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.18.6622 · Cited by 2,326
Counter, C. M., Avilion, A. A., LeFeuvre, C. E., Stewart, N. G., Greider, C. W., Harley, C. B., & Bacchetti, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05245.x · Cited by 2,096 · cited 2×
“clock controlling cell senescence (Counter et al., 1992; reviewed in Harley, 1995) and as a step in tumorigenesis Since DNA fragments with three, six or 12 telomeric”
BackgroundMorin, G. B. (1989) · Cell · doi:10.1016/0092-8674(89)90035-4 · Cited by 1,495
The locus of sequence-directed and protein-induced DNA bending
Wu, H., & Crothers, D. M. (1984) · Nature · doi:10.1038/308509a0 · Cited by 1,454
Control of telomere length by the human telomeric protein TRF1
van Steensel, B., & de Lange, T. (1997) · Nature · doi:10.1038/385740a0 · Cited by 1,219
Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast.
Guarente, L. P. (1983) · Methods in Enzymology · doi:10.1016/0076-6879(83)01013-7 · Cited by 1,022
A mutant with a defect in telomere elongation leads to senescence in yeast
Lundblad, V., & Szostak, J. W. (1989) · Cell · doi:10.1016/0092-8674(89)90132-3 · Cited by 931
Telomeres: Beginning to Understand the End
Zakian, V. A. (1995) · Science · doi:10.1126/science.270.5242.1601 · Cited by 859
Structure and variability of human chromosome ends.
de Lange, T., Shiue, L., Myers, R. M., Cox, D. R., Naylor, S. L., Killery, A. M., & Varmus, H. E. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.518 · Cited by 848
Research works printed but not linked: 4
- Blackburn EH (1993) Telomerase. In Gesteland,R.F. and Atkins,J.F. (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 557–576.
- Cooper J, Nimmo E, Allshire R and Cech T (1997) A Myb‐domain protein regulates telomere length and function in fission yeast. Nature, in press.
- de Lange T (1995) Telomere dynamics and genome instability in human cancer. In Blackburn,E.H. and Greider,C.W. (eds), Telomeres. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 265–295.
- Harley CB (1995) Telomeres and aging. In Blackburn,E.H. and Greider,C.W. (eds), Telomeres. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 247–265.
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Ghilain, C., Gilson, É., & Giraud-Panis, M.-J. E. (2024) · Wiley eBooks · doi:10.1002/9781394300808.ch3
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Williams, J. D., Tesmer, V. M., Kannoly, S., Shibuya, H., & Nandakumar, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.06.710105
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Marzec, P. (2013) · theses.fr (ABES) · doi:10.70675/2214c05fz9816z4523z8800zee5dcb9b9ff7
Kychygina, G. (2019) · theses.fr (ABES) · doi:10.70675/257216a4zfec4z40ccza35bz81fab5ab7e1e
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Chevalier, M. (2021) · theses.fr (ABES) · doi:10.70675/1b71e747zbcfbz428bzb910z90510832a61f
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Fages, J., Bergoglio, V., Julia, E., Cintori, L., Chailleux, C., Fourez, A.-L., Ponsolle, N., Trouche, D., & Canitrot, Y. (2026) · Cell Cycle · doi:10.1080/15384101.2026.2659192
Koeleman, E. S., Kaplan, C., Lima, M. A. D. R. B. F., Braun, D. M., Knotz, C., & Rippe, K. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.10.724127
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Buck, B., Weirich, A., Eramo, S., Lopez, R., White, L. K., Kabos, P., Forester, C., & Ramachandran, S. (2026) · Nature Communications · doi:10.1038/s41467-026-77352-z
Zhou, X., Wang, M., Hu, W., Chen, Z., Ma, W., Gao, B., Su, B., Wang, Y., Qin, J., Zhu, H., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01842-2
Hartmann, N. R. (2005) · MPG.PuRe (Max Planck Society)
Gao, H. (2006) · UA Campus Repository (The University of Arizona)
Functional Analysis of ACD Mutations in Dyskeratosis Congenita.
Koçak, H. (2014) · Deep Blue (University of Michigan)
Metadata
- Authors
- Bianchi, A., Smith, S., Chong, L., Elias, P., & de Lange, T.
- Affiliations
- Rockefeller University (US)
- ORCID
- Bianchi, Alessandro
- Venue
- The EMBO Journal
- Published
- 1997-04-01
- Volume
- 16
- Issue
- 7
- Pages
- 1785-1794
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- 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
- 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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