ATP-dependent allosteric DNA enzymes

Matthew Levy, Andrew D. Ellington

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Effector-activated ribozymes that respond to small organic molecules have previously been generated by appending binding species (aptamers) to ribozymes. In order to determine if deoxyribozymes can similarly be activated by effector molecules, we have appended an anti-adenosine aptamer to a selected deoxyribozyme ligase. The resultant constructs are specifically activated by ATP. Optimization of the joining region resulted in ligases that are activated up to 460-fold by ATP. The selected deoxyribozyme catalyzes ligation largely via a templating mechanism. Effector activation is surprisingly achieved by suppression of the rate of the background, templated ligation reaction in the absence of the effector molecule, probably by misalignment of the oligonucleotide substrates. This novel allosteric mechanism has not previously been observed for nucleic-acid catalysts and is rare even in protein catalysts.

Original languageEnglish (US)
Pages (from-to)417-426
Number of pages10
JournalChemistry and Biology
Volume9
Issue number4
DOIs
StatePublished - 2002
Externally publishedYes

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Catalytic DNA
Catalytic RNA
Adenosine Triphosphate
Ligases
Molecules
Ligation
DNA
Enzymes
Catalysts
Oligonucleotides
Joining
Adenosine
Nucleic Acids
Chemical activation
Substrates
Proteins

ASJC Scopus subject areas

  • Organic Chemistry

Cite this

ATP-dependent allosteric DNA enzymes. / Levy, Matthew; Ellington, Andrew D.

In: Chemistry and Biology, Vol. 9, No. 4, 2002, p. 417-426.

Research output: Contribution to journalArticle

Levy, Matthew ; Ellington, Andrew D. / ATP-dependent allosteric DNA enzymes. In: Chemistry and Biology. 2002 ; Vol. 9, No. 4. pp. 417-426.
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