A2 Refereed review article in a scientific journal
Structural modifications as tools in mechanistic studies of the cleavage of RNA phosphodiester linkages
Authors: Lönnberg Harri
Publisher: WILEY-V C H VERLAG GMBH
Publication year: 2022
Journal: Chemical Record
Journal name in source: CHEMICAL RECORD
Journal acronym: CHEM REC
Article number: e202200141
Number of pages: 18
ISSN: 1527-8999
eISSN: 1528-0691
DOI: https://doi.org/10.1002/tcr.202200141
Web address : https://doi.org/10.1002/tcr.202200141
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/176120341
The cleavage of RNA phosphodiester bonds by RNase A and hammerhead ribozyme at neutral pH fundamentally differs from the spontaneous reactions of these bonds under the same conditions. While the predominant spontaneous reaction is isomerization of the 3',5'-phosphodiester linkages to their 2',5'-counterparts, this reaction has never been reported to compete with the enzymatic cleavage reaction, not even as a minor side reaction. Comparative kinetic measurements with structurally modified di-nucleoside monophosphates and oligomeric phosphodiesters have played an important role in clarification of mechanistic details of the buffer-independent and buffer-catalyzed reactions. More recently, heavy atom isotope effects and theoretical calculations have refined the picture. The primary aim of all these studies has been to form a solid basis for mechanistic analyses of the action of more complicated catalytic machineries. In other words, to contribute to conception of a plausible unified picture of RNA cleavage by biocatalysts, such as RNAse A, hammerhead ribozyme and DNAzymes. In addition, structurally modified trinucleoside monophosphates as transition state models for Group I and II introns have clarified some features of the action of large ribozymes.
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