Cooperative binding of effectors by an allosteric ribozyme

Antony M. Jose, Garrett A. Soukup, Ronald R. Breaker

Research output: Contribution to journalArticlepeer-review

81 Scopus citations


An allosteric ribozyme that requires two different effectors to induce catalysis was created using modular rational design. This ribozyme construct comprises five conjoined RNA modules that operate in concert as an obligate FMN- and theophylline-dependent molecular switch. When both effectors are present, this 'binary' RNA switch self-cleaves with a rate enhancement of ∼300-fold over the rate observed in the absence of effectors. Kinetic and structural studies implicate a switching mechanism wherein FMN binding induces formation of the active ribozyme conformation. However, the binding site for FMN is rendered inactive unless theophylline first binds to its corresponding site and reorganizes the RNA structure. This example of cooperative binding between allosteric effectors reveals a level of structural and functional complexity for RNA that is similar to that observed with allosteric proteins.

Original languageEnglish (US)
Pages (from-to)1631-1637
Number of pages7
JournalNucleic Acids Research
Issue number7
StatePublished - Apr 1 2001

All Science Journal Classification (ASJC) codes

  • Genetics


Dive into the research topics of 'Cooperative binding of effectors by an allosteric ribozyme'. Together they form a unique fingerprint.

Cite this