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‘Intelligent’ ribozyme whose activity is altered in response to K + as a result of quadruplex formation
Author(s) -
Nagata Takashi,
Sakurai Yu,
Hara Yukari,
Mashima Tsukasa,
Kodaki Tsutomu,
Katahira Masato
Publication year - 2012
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2012.08538.x
Subject(s) - ribozyme , chemistry , linker , hammerhead ribozyme , residue (chemistry) , catalysis , biophysics , mammalian cpeb3 ribozyme , stereochemistry , rna , microbiology and biotechnology , biochemistry , biology , gene , computer science , operating system
The structure of r(GGAGGAGGAGGA) (R12) changes from a single‐stranded form to a compact quadruplex one in response to K + . In a hammerhead ribozyme, two portions of the catalytic core are linked with the stem and are located in close proximity in order to exert activity. In this study, the stem was replaced by R12 (or R11, which lacks the terminal A residue) with or without linker residues. One of the newly constructed ribozymes exhibited enhanced activity in response to K + , and we suggest that quadruplex formation restored the active catalytic core. Other ribozymes exhibited repressed activity in response to K + , suggesting that formation of the active core was prevented. Thus, we have succeeded in developing ‘intelligent’ ribozymes whose activity is either repressed or enhanced in response to K + . This switching capability may have therapeutic applications because of the differences between intra‐ and extracellular K + concentrations.