Nucleic Acids Research, 1991, Vol. 19, No. 7 1605-1612
© 1991
MOLECULAR BIOLOGY |
Ribonuclease T1 generates circular RNA molecules from viroid-specific RNA transcripts by cleavage and intramolecular ligation
1Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology PO Box 1527, GR-711 10 Heraklion, Crete, Greece 2Max-Planck-Institut für Biochemie Abteilung Viroidforschung, D-8033 Planegg-Martinsried, FRG
* To whom correspondence should be addressed
Received November 22, 1990. Revised February 28, 1991. Accepted February 28, 1991.
A 406 nucleotide long potato spindle tuber virold (PSTVd)-specffic linear RNA transcript was synthesized in vitro and subjected to limited digestion with ribonuclease (RNase) T1. Under certain conditions this guanosine-specific endoribonuclease proved to be capable of processing the longer-than-unit-length, precursor-like viroid RNA transcript by cleaving out a linear 358 nucleotide long product and ligating that to a circular RNA molecule. The new finding that RNase T1 acts as an RNA processing enzyme and, in particular, as an RNA ‘circulase’ can be explained by the unique structural preconditions inherent in the viroid-specific substrate and by the well characterized two-step cleavage mechanism of the enzyme. These in vitro potentials of RNase T1 suggest that also in vivo procaryotic and eucaryotic RNases with a similar reaction mechanism might not only be involved in RNA degradation and trimming, but also in processing, ligation and recombination of RNA.
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