Cited by 292CRISPR and Genetic EngineeringRNA Interference and Gene DeliveryDNA and Nucleic Acid Chemistry

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In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence

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Choo, Yen, Sánchez-García, Isidro, Klug, Aaron·1994·Nature

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Abstract

A DNA-binding peptide comprising three zinc-fingers has been engineered to bind specifically to a unique nine-base-pair region of a BCR-ABL fusion oncogene in preference to the parent genomic sequences. Binding to the target oncogene in chromosomal DNA is possible in transformed cells in culture, and results in blockage of transcription. Consequently, murine cells rendered independent of growth factors by the action of the oncogene revert to factor dependence upon transient transfection with a vector expressing the peptide.

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Fusion Proteins Consisting of Human Immunodeficiency Virus Type 1 Integrase and the Designed Polydactyl Zinc Finger Protein E2C Direct Integration of Viral DNA into Specific Sites
Tan, W., Zhu, K., Segal, D., Barbas, C., & Chow, S. A. (2004) · Journal of Virology · doi:10.1128/jvi.78.3.1301-1313.2004 · Cited by 90
“Artificial transcription factors based on modified zinc finger domains have been used to target specific DNA sequences and selectively activate or repress expression of reporter genes (4, 5, 10, 12, 16, 28, 32, 33, 37, 47).”
Background
MDR1 Promoter Hypermethylation in MCF-7 Human Breast Cancer Cells: Changes in Chromatin Structure Induced by Treatment with 5-Aza-Cytidine
David, G. L., Yegnasubramanian, S., Kumar, A., Marchi, V. L., Marzo, A. M. D., Lin, X., & Nelson, W. G. (2004) · Cancer Biology & Therapy · doi:10.4161/cbt.3.6.845 · Cited by 88
Sequence specificity is obtained from the majority of modular C2H2 zinc-finger arrays
Lam, K. N., van Bakel, H., Coté, A. G., van der Ven, A., & Hughes, T. R. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1303 · Cited by 86
“The evolutionary success of C2H2-ZFs may also be explained in part by their capacity for modular assembly: individual C2H2-ZFs (‘modules’) can be recombined to produce proteins (Zinc Finger Arrays, or ZFAs) with new binding specificities, and both natural and artificial C2H2-ZFs have been used successfully in modular…”
Background
In vivo inhibition by a site-specific catalytic RNA subunit of RNase P designed against the BCR-ABL oncogenic products: a novel approach for cancer treatment
Cobaleda, C., & Sánchez-Garcı́a, I. (2000) · Blood · doi:10.1182/blood.v95.3.731.003k28_731_737 · Cited by 86
Self-citation
The rise of DNA methylation and the importance of chromatin on multidrug resistance in cancer
Baker, E. K., & El‐Osta, A. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00342-2 · Cited by 85
Targeting CCR5 as a Component of an HIV-1 Therapeutic Strategy
Mohamed, H., Gurrola, T., Berman, R., Collins, M., Sariyer, I. K., Nonnemacher, M. R., & Wigdahl, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.816515 · Cited by 81
Recent developments in the engineering of zinc finger proteins
Moore, M., & Ullman, C. G. (2003) · Briefings in Functional Genomics · doi:10.1093/bfgp/1.4.342 · Cited by 81
Arresting Cancer Proliferation by Small-Molecule Gene Regulation
Dickinson, L. A., Burnett, R., Melander, C., Edelson, B. S., Arora, P. S., Dervan, P. B., & Gottesfeld, J. M. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.09.004 · Cited by 81
Imaging Specific Genomic DNA in Living Cells
Chen, B., Guan, J., & Huang, B. (2016) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-062215-010830 · Cited by 77
“Each zinc finger can be engineered to recognize a nucleotide triplet (71, 110) and several fingers can be arranged in tandem as a zinc-finger protein (ZFP) to recognize a broad spectrum of DNA sequences with high specificity (29, 107).”
Background
Chemical Approaches to Control Gene Expression
Gottesfeld, J. M., Turner, J. M., & Dervan, P. B. (2001) · Gene Expression · doi:10.3727/000000001783992696 · Cited by 80
Overlap of Nuclear Localisation Signal and Specific DNA-binding Residues Within the Zinc Finger Domain of PacC
Fernández-Martı́nez, J., Brown, C. V., Dı́ez, E., Tilburn, J., Arst, H. N., Peñalva, M. A., & Espeso, E. A. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.072 · Cited by 76
Inhibition of herpes simplex virus 1 gene expression by designer zinc-finger transcription factors
Papworth, M. A., Moore, M., Isalan, M., Minczuk, M. A., Choo, Y., & Klug, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252773399 · Cited by 76
Self-citation
Characterisation of site-biased DNA methyltransferases: specificity, affinity and subsite relationships
McNamara, A. R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf501 · Cited by 74
“The gene encoding the three zinc ®nger protein recognising the 9 bp sequence 5¢-GCAGAAGCC-3¢ (22) was a generous gift from Dr Yen Choo (LMB, University of Cambridge, UK).”
Method
Towards therapeutic applications of engineered zinc finger proteins
Klug, A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.104 · Cited by 74
Self-citation
Repression of vascular endothelial growth factor A in glioblastoma cells using engineered zinc finger transcription factors.
Snowden, A. W., Zhang, L., Urnov, F. D., Dent, C. L., Jouvenot, Y., Zhong, X., Rebar, E. J., Jamieson, A. C., Zhang, H. S., Tan, S., et al. (2003) · PubMed · Cited by 71
Determining the Specificities of TALENs, Cas9, and Other Genome-Editing Enzymes
Pattanayak, V., Guilinger, J. P., & Liu, D. R. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801185-0.00003-9 · Cited by 70
Phase display of proteins
Dunn, I. S. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80060-7 · Cited by 70
Design of polyzinc finger peptides with structured linkers
Moore, M., Choo, Y., & Klug, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1432 · Cited by 69
Self-citation
Towards an understanding of protein-DNA recognition
Rhodes, D., Schwabe, J. W. R., Chapman, A. C., & Fairall, L. (1996) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1996.0048 · Cited by 69
Gene editing and its applications in biomedicine
Li, G., Li, X., Zhuang, S., Wang, L., Zhu, Y., Chen, Y., Sun, W. C., Wu, Z., Zhou, Z. L., Chen, J., et al. (2022) · Science China Life Sciences · doi:10.1007/s11427-021-2057-0 · Cited by 66
“Gene editing in primary T cells for immunotherapy In 1994, zinc finger proteins were first shown to repress the function of oncogenic BCR-ABL fusion sequences by directly binding DNA (Choo et al., 1994).”
Background
Changing the Structural Context of a Functional β-Hairpin
Drakopoulou, E., Zinn‐Justin, S., Guenneugues, M., Gilquin, B., Ménèz, A., & Vita, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.20.11979 · Cited by 68
Designing DNA-binding proteins on the surface of filamentous phage
Choo, Y., & Klug, A. (1995) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(95)80073-5 · Cited by 68
Self-citation
Targeted Methylation of the Epithelial Cell Adhesion Molecule (EpCAM) Promoter to Silence Its Expression in Ovarian Cancer Cells
Nunna, S., Reinhardt, R., Ragozin, S., & Jeltsch, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087703 · Cited by 65
“Since Zinc fingers were the first protein modules for which design of sequence specific DNA binding became possible [53–58], initial targeted methylation studies relied on artificial zinc-finger proteins as targeting device [59].”
Altered DNA-binding specificity mutants of EKLF and Sp1 show that EKLF is an activator of the β-globin locus control region in vivoPreprint
Gillemans, N., Tewari, R., Lindeboom, F., Rottier, R. J., de Wit, T., Wijgerde, M., Grosveld, F. G., & Philipsen, S. (1998) · Genes & Development · doi:10.1101/gad.12.18.2863 · Cited by 65
“Furthermore, an engineered zinc finger domain recognizing a unique region of the BCR– ABL fusion oncogene has been shown to impair the expression of this oncogene in transformed cells after transient transfection in culture (Choo et al. 1994).”
Background
Epigenetic Editing: On the Verge of Reprogramming Gene Expression at Will
Cano-Rodríguez, D., & Rots, M. G. (2016) · Current Genetic Medicine Reports · doi:10.1007/s40142-016-0104-3 · Cited by 66
“binding domain without any effector domain to promoter regions or regions downstream of the transcription start site can silence gene expression by steric hindrance of transcription factors and RNA polymerase [46, 57].”
Background

Authors: Choo, Y., Sánchez-García, I., & Klug, A.
Affiliations: MRC Laboratory of Molecular Biology (GB)
ORCID: Choo, Yen
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1994-12
Volume: 372
Issue: 6507
Pages: 642-645
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/372642a0
OpenAlex: W2019616754
Cited by: 292
References: 36
Citations by year: 2026: 1 · 2025: 4 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 9 · 2019: 3 · 2018: 3 · 2017: 7 · 2016: 9 · 2015: 9 · 2014: 11 · 2013: 1 · 2012: 6
FWCI: 7.35
Type: journal article
Language: en
Open access: green
hdl.handle.net
Licence: other-oa
www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, other-oa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords: zinc finger DNA-binding protein, transcriptional repression, site-specific DNA binding, growth factor independence, transformed cells, transcriptional block
MeSH terms: Amino Acid Sequence, Animals, Cell Line, DNA, DNA-Binding Proteins, Feasibility Studies, Gene Expression Regulation, Humans, Molecular Sequence Data, Protein Binding, Recombinant Fusion Proteins, Transcription, Genetic, Transfection, Fusion Proteins, bcr-abl, Zinc Fingers, Mice

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In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence

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