Abstract
We consider the autocatalytic synthesis of MDV-1 RNA by Q beta replicase, which proceeds by template-instructed replication. We predict the effect of a particular point mutation in the sequence on the overall doubling time and conjecture its role on the recognition step. The mutation considered destabilizes the folding of the internal recognition site. The theoretical analysis is based on the calculation of nonequilibrium re-folding events which occur in the RNA chains as they are being synthesized. Free-energy minima are irrelevant. In order to test the theoretical findings, we incubate both the natural template and the mutant simultaneously, in the presence of the replicase. The experiment reveals that the mutation facilitates the enzyme-template interaction, thus enhancing recognition. However, examining the exponential phase of the replication kinetics, where the enzyme is in large excess with respect to the RNA species, we can conclude that the mutant presents a larger overall doubling time, in good agreement with our theoretical findings.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Berichte der Bunsengesellschaft für physikalische Chemie
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
