Related Experiment Video
Updated: Aug 15, 2026

Nanomanipulation of Single RNA Molecules by Optical Tweezers
Published on: August 20, 2014
Mechanism for allosteric inhibition of an ATP-sensitive ribozyme
1Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA.
Abstract:
We report the structural basis for the modulation of an ATP-sensitive ribozyme that was engineered by modular rational design. This allosteric ribozyme is composed of two independently functioning domains, one a receptor for ATP and the other a self-cleaving ribozyme. When fused in the appropriate fashion, the conjoined aptamer-ribozyme construct functions as an allosteric ribozyme that is inhibited in the presence of ATP. The aptamer domain remains conformationally heterogeneous in the absence of ATP, but folds into a distinct structure upon ligand binding. This ATP-induced conformational change causes a reduction in catalytic activity of the adjacent ribozyme domain due to steric interference between the aptamer and ribozyme tertiary structures. This mechanism for structural and functional modulation of nucleic acids is one of several possible mechanisms by which the function of ribozymes could be specifically controlled by small effector molecules.
Related Concept Videos
Allosteric Regulation
Allosteric Regulation
Riboswitches
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Ribozymes
Ribozymes can be...
Ribozymes
Ribozymes can be...
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

