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Mol Cell Biol. 2010 Jul;30(13):3142-50. doi: 10.1128/MCB.00300-10. Epub 2010 Apr 26.

R2 retrotransposons encode a self-cleaving ribozyme for processing from an rRNA cotranscript.

Author information

1
Department of Biology, University of Rochester, Rochester, NY 14627, USA. eick@mail.rochester.edu

Abstract

The non-long terminal repeat (non-LTR) retrotransposon R2 is inserted into the 28S rRNA genes of many animals. Expression of the element appears to be by cotranscription with the rRNA gene unit. We show here that processing of the rRNA cotranscript at the 5' end of the R2 element in Drosophila simulans is rapid and utilizes an unexpected mechanism. Using RNA synthesized in vitro, the 5' untranslated region of R2 was shown capable of rapid and efficient self-cleavage of the 28S-R2 cotranscript. The 5' end generated in vitro by the R2 ribozyme was at the position identical to that found for in vivo R2 transcripts. The RNA segment corresponding to the R2 ribozyme could be folded into a double pseudoknot structure similar to that of the hepatitis delta virus (HDV) ribozyme. Remarkably, 21 of the nucleotide positions in and around the active site of the HDV ribozyme were identical in R2. R2 elements from other Drosophila species were also shown to encode HDV-like ribozymes capable of self-cleavage. Tracing their sequence evolution in the Drosophila lineage suggests that the extensive similarity of the R2 ribozyme from D. simulans to that of HDV was a result of convergent evolution, not common descent.

PMID:
20421411
PMCID:
PMC2897577
DOI:
10.1128/MCB.00300-10
[Indexed for MEDLINE]
Free PMC Article

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