The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
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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In the citing paper
“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
In the citing paper
“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
Citations
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
Cited by
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The depth of chemical time and the power of enzymes as catalysts.
Wolfenden, R., & Snider, M. (2001) · Accounts of Chemical Research · doi:10.1021/ar000058i · Cited by 823
DNA Recognition by Cys2His2 Zinc Finger Proteins
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
Design and Selection of Novel Cys2His2 Zinc Finger Proteins
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
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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