The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Defining the sequence specificity of DNA-binding proteins by selecting binding sites from random-sequence oligonucleotides: analysis of yeast GCN4 protein.
Open accessAbstract
We describe a new method for accurately defining the sequence recognition properties of DNA-binding proteins by selecting high-affinity binding sites from random-sequence DNA. The yeast transcriptional activator protein GCN4 was coupled to a Sepharose column, and binding sites were isolated by passing short, random-sequence oligonucleotides over the column and eluting them with increasing salt concentrations. Of 43 specifically bound oligonucleotides, 40 contained the symmetric sequence TGA(C/G)TCA, whereas the other 3 contained sequences matching six of these seven bases. The extreme preference for this 7-base-pair sequence suggests that each position directly contacts GCN4. The three nucleotide positions on each side of this core heptanucleotide also showed sequence preferences, indicating their effect on GCN4 binding. Interestingly, deviations in the core and a stronger sequence preference in the flanking region were found on one side of the central C . G base pair. Although GCN4 binds as a dimer, this asymmetry supports a model in which interactions on each side of the binding site are not equivalent. The random selection method should prove generally useful for defining the specificities of other DNA-binding proteins and for identifying putative target sequences from genomic DNA.
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Cites
Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA Polymerase
Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B., & Erlich, H. A. (1988) · Science · doi:10.1126/science.2448875 · Cited by 17,719
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
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Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing
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Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis
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Affinity purification of sequence-specific DNA binding proteins.
Kadonaga, J. T., & Tjian, R. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.16.5889 · Cited by 1,154
Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of Yeast
Hope, I. A., & Struhl, K. (1986) · Cell · doi:10.1016/0092-8674(86)90070-x · Cited by 880
Self-citationA new class of yeast transcriptional activators
Ma, J., & Ptashne, M. (1987) · Cell · doi:10.1016/0092-8674(87)90015-8 · Cited by 687
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Cited by
Ellenberger, T. E., Brandl, C. J., Struhl, K., & Harrison, S. C. (1992) · Cell · doi:10.1016/s0092-8674(05)80070-4 · Cited by 972
Self-citationHITS-CLIP: panoramic views of protein-RNA regulation in living cells
Darnell, R. B. (2010) · WIREs RNA · doi:10.1002/wrna.31 · Cited by 382
UniPROBE: an online database of protein binding microarray data on protein-DNA interactions
Newburger, D. E., & Bulyk, M. L. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn660 · Cited by 367
SELEX: Critical factors and optimization strategies for successful aptamer selection
Kohlberger, M., & Gadermaier, G. (2022) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2244 · Cited by 341
Deciphering eukaryotic gene-regulatory logic with 100 million random promoters
de Boer, C. G., Vaishnav, E. D., Sadeh, R., Abeyta, E. L., Friedman, N., & Regev, A. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0315-8 · Cited by 283
Metadata
- Authors
- Oliphant, A. R., Brandl, C. J., & Struhl, K.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1989-07
- Volume
- 9
- Issue
- 7
- Pages
- 2944-2949
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2125819516
- Cited by
- 357
- References
- 21
- FWCI
- 6.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Oliphant, A. R., Brandl, C. J., & Struhl, K. (1989). Defining the sequence specificity of DNA-binding proteins by selecting binding sites from random-sequence oligonucleotides: analysis of yeast GCN4 protein. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.9.7.2944
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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