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A DNA Aptamer That Binds Adenosine and ATP
Abstract
We have used in vitro selection to isolate adenosine/ATP-binding DNA sequences from a pool of approximately 2 x 10(14) different random-sequence single-stranded DNA molecules. One of these aptamers has been characterized and binds adenosine in solution with a dissociation constant of 6 +/- 3 microM. Experiments with ATP analogs indicate that functional groups on both the base and the sugar of ATP are involved in the ligand/aptamer interaction. The binding domain of this aptamer was localized to a 42 base sequence by deletion analysis. A pool of mutagenized versions of this sequence was then synthesized and screened for functional adenosine binding sequences; comparison of the selected variants revealed two highly conserved guanosine-rich regions, two invariant adenosine residues, and two regions of predominantly Watson--Crick covariation. This data led us to propose a model of the ATP-binding DNA structure which is based on a stable framework composed of two stacked G-quartets. The two highly conserved adenosine residues may stack between the top G-quartet and the two short stems, forming a pocket in which the adenosine or ATP ligand binds. Site-directed mutagenesis, base analog substitution studies, and the design of highly divergent but functional sequences provide support for this model.
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Cites
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Metadata
- Authors
- Huizenga, D. E., & Szostak, J. W.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-01-01
- Volume
- 34
- Issue
- 2
- Pages
- 656-665
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1970478438
- Cited by
- 1,270
- References
- 1
- FWCI
- 6.39
- Type
- journal article
- Language
- en
- Open access
- closed
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