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Structure-Based Design of Transcription Factors
Abstract
Computer modeling suggested that transcription factors with novel sequence specificities could be designed by combining known DNA binding domains. This structure-based strategy was tested by construction of a fusion protein, ZFHD1, that contained zinc fingers 1 and 2 from Zif268, a short polypeptide linker, and the homeodomain from Oct-1. The fusion protein bound optimally to a sequence containing adjacent homeodomain (TAATTA) and zinc finger (NGGGNG) subsites. When fused to an activation domain, ZFHD1 regulated promoter activity in vivo in a sequence-specific manner. Analysis of known protein-DNA complexes suggests that many other DNA binding proteins could be designed in a similar fashion.
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“Previous studies have either created chimeric transcription factors which recognize synthetic regulatory elements by fusing domains from biologically unrelated proteins, or used phage display technology to create a zinc finger protein which recognizes a DNA site generated by a chromosomal translocation”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Pomerantz et al., 1995
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“This is consistent with the overall selectivity of a chimeric transcription factor depending on the intermediate affinity and high specificity of the isolated sub-domains”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Pomerantz et al., 1995
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Cites
Zinc Finger-DNA Recognition: Crystal Structure of a Zif268-DNA Complex at 2.1 Å
Pavletich, N. P., & Pabo, C. O. (1991) · Science · doi:10.1126/science.2028256 · Cited by 2,081
Self-citationCrystallographic analysis of the interaction of the glucocorticoid receptor with DNA
Luisi, B. F., Xu, W. X., Otwinowski, Z., Freedman, L. P., Yamamoto, K. R., & Sigler, P. B. (1991) · Nature · doi:10.1038/352497a0 · Cited by 1,503
On the attribution and additivity of binding energies
Jencks, W. P. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4046 · Cited by 938
Christy, B. A., Lau, L. F., & Nathans, D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.7857 · Cited by 734
The ubiquitous octamer-binding protein Oct-1 contains a POU domain with a homeo box subdomain.Preprint
Sturm, R. A., Das, G., & Herr, W. (1988) · Genes & Development · doi:10.1101/gad.2.12a.1582 · Cited by 639
Klemm, J. D., Rould, M. A., Aurora, R., Herr, W., & Pabo, C. O. (1994) · Cell · doi:10.1016/0092-8674(94)90231-3 · Cited by 506
Self-citationPhilip, C. M., Rould, M. A., Weintraub, H. M., & Pabo, C. O. (1994) · Cell · doi:10.1016/0092-8674(94)90159-7 · Cited by 461
Self-citationZinc Finger Phage: Affinity Selection of Fingers with New DNA-Binding Specificities
Rebar, E. J., & Pabo, C. O. (1994) · Science · doi:10.1126/science.8303274 · Cited by 417
Self-citationDNA binding specificity of homeodomains
Laughon, A. S. (1991) · Biochemistry · doi:10.1021/bi00112a001 · Cited by 284
The DNA binding specificity of the bipartite POU domain and its subdomains.
Verrijzer, C. P., Alkema, M. J., van Weperen, W. W., van Leeuwen, H. C., Strating, M., & van der Vliet, P. C. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05606.x · Cited by 266
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Wolfe, S. A., Nekludova, L., & Pabo, C. O. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.183 · Cited by 1,053
Self-citationMolecular Recognition of Protein−Ligand Complexes: Applications to Drug Design
Babine, R. E., & Bender, S. L. (1997) · Chemical Reviews · doi:10.1021/cr960370z · Cited by 889
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Pabo, C. O., Peisach, E., & Grant, R. A. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.313 · Cited by 733
Self-citationRuffell, D., Mourkioti, F., Gambardella, A., Kirstetter, P., Lopez, R. G., Rosenthal, N., & Nerlov, C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908641106 · Cited by 626
Sawaya, M. R., Prasad, R., Wilson, S. H., Kraut, J., & Pelletier, H. (1997) · Biochemistry · doi:10.1021/bi9703812 · Cited by 593
Li, Y., & Breaker, R. R. (1999) · Journal of the American Chemical Society · doi:10.1021/ja990592p · Cited by 587
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Rivera, V. M., Clackson, T., Natesan, S., Pollock, R. M., Amara, J. F., Keenan, T. P., Magari, S. R., Phillips, T., Courage, N. L., Cerasoli, F., et al. (1996) · Nature Medicine · doi:10.1038/nm0996-1028 · Cited by 528
Noyes, M. B., Christensen, R. G., Wakabayashi, A., Stormo, G. D., Brodsky, M. H., & Wolfe, S. A. (2008) · Cell · doi:10.1016/j.cell.2008.05.023 · Cited by 452
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BackgroundRadzicka, A., & Wolfenden, R. (1996) · Journal of the American Chemical Society · doi:10.1021/ja954077c · Cited by 484
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Elrod-Erickson, M., Rould, M. A., Nekludova, L., & Pabo, C. O. (1996) · Structure · doi:10.1016/s0969-2126(96)00125-6 · Cited by 421
“[4–10]).”
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Greisman, H. A., & Pabo, C. O. (1997) · Science · doi:10.1126/science.275.5300.657 · Cited by 331
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Liu, Q., Segal, D. J., Ghiara, J. B., & Barbas, C. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5525 · Cited by 288
Computational prediction of transcription-factor binding site locations.
Bulyk, M. L. (2003) · Genome biology · doi:10.1186/gb-2003-5-1-201 · Cited by 314
“These approaches have come either from analysis of databases of well-characterized DNA-protein interactions [108-112], from computer modeling [113,114], or from experiments employing in vitro selection from a randomized library, either of the DNA base pairs or the amino-acid residues implicated in…”
MethodDahiyat, B. I., & Mayo, S. L. (1996) · Protein Science · doi:10.1002/pro.5560050511 · Cited by 302
“Among non de novo approaches, domains of naturally occurring proteins have been modified or coupled together to achieve a desired tertiary organization (Pessi et al., 1993; Pomerantz et al., 1995).”
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Wolfenden, R. V., Lu, X., & Young, G. B. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9813055 · Cited by 274
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Robinson, C. R., & Sauer, R. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5929 · Cited by 271
Jin, Y., & Cowan, J. A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0503985 · Cited by 252
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Guyomarc’H, F., Law, A. J. R., & Dalgleish, D. G. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0211783 · Cited by 224
Kim, J., & Pabo, C. O. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2812 · Cited by 221
Self-citationBrass, A. L., Zhu, A. Q., & Singh, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.977 · Cited by 204
“…factors which recognize synthetic regulatory elements by fusing domains from biologically unrelated proteins, or used phage display technology to create a zinc finger protein which recognizes a DNA site generated by a chromosomal translocation (Choo et al., 1994; Pomerantz et al., 1995).”
BackgroundPromoter Specificity and Biological Activity of Tethered AP-1 Dimers
Bakiri, L., Matsuo, K., Wisniewska, M. B., Wagner, E. F., & Yaniv, M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4952-4964.2002 · Cited by 205
“it more disruptive than dimerization domain swapping or mutagenesis in order to restrict dimerization to one or more partners (1, 4, 31, 37).”
BackgroundA versatile synthetic dimerizer for the regulation of protein–protein interactions
Amara, J. F., Clackson, T., Rivera, V. M., Guo, T., Keenan, T. P., Natesan, S., Pollock, R. M., Wu, Y., Courage, N. L., Holt, D. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10618 · Cited by 205
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Rollins, C. T., Rivera, V. M., Woolfson, D. N., Keenan, T. P., Hatada, M. H., Adams, S. E., Andrade, L. J., Yaeger, D., van Schravendijk, M. R., Holt, D. A., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100101997 · Cited by 189
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Noyes, M. B., Meng, X., Wakabayashi, A., Sinha, S., Brodsky, M. H., & Wolfe, S. A. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn048 · Cited by 171
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Hegg, E. L., & Burstyn, J. N. (1996) · Inorganic Chemistry · doi:10.1021/ic960384n · Cited by 147
Warshel, A., Štrajbl, M., Villà-Freixa, J., & Florián, J. (2000) · Biochemistry · doi:10.1021/bi000987h · Cited by 140
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“Therefore, fusing FKBP12 and mTOR with a DNA-binding domain of ZFHD1 [51] and the activation domain of NF-κB p65 protein [52], respectively, bridges both domains to drive expression of the gene Cells 2019, 8, 796 6 of 16 of interest in a rapamycin-dependent fashion (Figure 3A) [46].”
BackgroundWolfenden, R. V., Ridgway, C. G., & Young, G. B. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9733604 · Cited by 130
Desbiez, C., David, C., Mettouchi, A., Laufs, J., & Gronenborn, B. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5640 · Cited by 129
Highly Specific DNA Recognition by a Designed Miniature Protein
Zondlo, N. J., & Schepartz, A. (1999) · Journal of the American Chemical Society · doi:10.1021/ja990968z · Cited by 129
Kollman, P. A., Kuhn, B., Donini, O., Peräkylä, M., Stanton, R., & Bakowies, D. (2000) · Accounts of Chemical Research · doi:10.1021/ar000032r · Cited by 125
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Rossi, F. M. V., & Blau, H. M. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80028-1 · Cited by 113
Palmer, D. R. J., Garrett, J. B., Sharma, V., Meganathan, R., Babbitt, P. C., & Gerlt, J. A. (1999) · Biochemistry · doi:10.1021/bi990140p · Cited by 114
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Qiao, L., Murray, B. W., Shimazaki, M., Schultz, J., & Wong, C. (1996) · Journal of the American Chemical Society · doi:10.1021/ja960274f · Cited by 105
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Jamieson, A. C., Wang, H., & Kim, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.12834 · Cited by 103
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Amyes, T. L., Richard, J. P., & Tait, J. J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja055493s · Cited by 102
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Harris, P., Poulsen, J.-C. N., Jensen, K. F., & Larsen, S. (2000) · Biochemistry · doi:10.1021/bi992952r · Cited by 95
Major, D. T., & Gao, J.-L. (2007) · Journal of Chemical Theory and Computation · doi:10.1021/ct600371k · Cited by 24
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Clackson, T. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80012-9 · Cited by 88
Cho, H., Choi, G., Choi, K. Y., & Oh, B. (1998) · Biochemistry · doi:10.1021/bi9801614 · Cited by 82
Zabinski, R. F., & Toney, M. D. (2000) · Journal of the American Chemical Society · doi:10.1021/ja0026354 · Cited by 81
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Iwahara, J., Schwieters, C. D., & Clore, G. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja046246b · Cited by 79
Amyes, T. L., Wood, B. M., Chan, K. K., Gerlt, J. A., & Richard, J. P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710384t · Cited by 77
Tanaka, F., Fuller, R. P., & Barbas, C. F. (2005) · Biochemistry · doi:10.1021/bi050216j · Cited by 76
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Bryant, R. A. R., & Hansen, D. E. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953137b · Cited by 75
Kim, S. P., Leach, A. G., & Houk, K. N. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo011180d · Cited by 75
Marasco, W. (1995) · Immunotechnology · doi:10.1016/1380-2933(95)00001-1 · Cited by 75
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BackgroundMcNamara, A. R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf501 · Cited by 74
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Sugahara, T., Sato, A., 工藤, 正., Ben-Menahem, D., Pixley, M. R., Hsueh, A. J. W., & Boime, I. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10445 · Cited by 73
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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
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Wolfe, S., Ramm, E. I., & Pabo, C. (2000) · Structure · doi:10.1016/s0969-2126(00)00161-1 · Cited by 63
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Kusakabe, T., & Richardson, C. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19563 · Cited by 62
Bearne, S. L., & Wolfenden, R. V. (1997) · Biochemistry · doi:10.1021/bi9620722 · Cited by 61
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Pomerantz, J. L., Wolfe, S. A., & Pabo, C. O. (1998) · Biochemistry · doi:10.1021/bi972464o · Cited by 60
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Tycko, J., Van, M. V., Aradhana, DelRosso, N., Ye, H., Yao, D., Valbuena, R., Vaughan-Jackson, A., Xu, X., Ludwig, C., et al. (2025) · Nature Biotechnology · doi:10.1038/s41587-024-02442-6 · Cited by 57
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Melkko, S., Dumelin, C. E., Scheuermann, J., & Neri, D. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.12.006 · Cited by 56
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Corbi, N., Libri, V., Fanciulli, M., Tinsley, J. M., Davies, K., & Passananti, C. (2000) · Gene Therapy · doi:10.1038/sj.gt.3301204 · Cited by 56
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Metadata
- Authors
- Pomerantz, J. L., Sharp, P. A., & Pabo, C. O.
- Affiliations
- Harvard–MIT Division of Health Sciences and Technology (US)
- Massachusetts Institute of Technology (US)
- Venue
- Science
- Published
- 1995-01-06
- Volume
- 267
- Issue
- 5194
- Pages
- 93-96
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2022704908
- Cited by
- 226
- References
- 18
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 1 · 2022: 2 · 2019: 1 · 2018: 2 · 2017: 4 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 2
- FWCI
- 9.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (P01CA042063, P30CA014051)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
- Keywords
- structure-based protein design, DNA-binding domain, zinc finger, homeodomain, Zif268, Oct-1, fusion protein, sequence specificity, protein-DNA complex, promoter regulation, transactivation domain
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Cloning, Molecular, Computer Simulation, DNA-Binding Proteins, Gene Expression Regulation, Models, Molecular, Molecular Sequence Data, Promoter Regions, Genetic, Recombinant Fusion Proteins, Transcription Factors, Transfection, Protein Engineering, Zinc Fingers, Homeodomain Proteins, Octamer Transcription Factor-1, Host Cell Factor C1
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