Journal article

A DNA Aptamer That Binds Adenosine and ATP

Huizenga D, Szostak J ...see all

Biochemistry, vol. 34, issue 2 (1995) pp. 656-665

  • 235


    Mendeley users who have this article in their library.
  • 681


    Citations of this article.
  • N/A


    ScienceDirect users who have downloaded this article.
Sign in to save reference


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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text


  • David E. Huizenga

  • Jack W. Szostak

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free