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J. Biol. Chem., Vol. 277, Issue 38, 34836-34845, September 20, 2002
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From the Department of Biology, University of Rochester,
Rochester, New York 14627-0211
R2 is a retrotransposable element that
specifically inserts into the 28 S rRNA genes of arthropods. The
element encodes a single protein with endonuclease activity that
cleaves the 28 S gene target site and reverse transcriptase (RT)
activity that uses the cleaved DNA to prime reverse transcription. Here
we compare various properties of the R2 RT activity with those
of the well characterized retroviral RT, avian myeloblastosis virus
(AMV). In processivity assays using heterogeneous RNA templates, R2 RT can synthesize cDNA over twice the length of that synthesized by
AMV RT and can synthesize cDNA over 4 times longer than AMV RT in
assays with poly(rA) templates. The higher processivity of R2 RT
compared with retroviral RTs is a result of the slower rate of
dissociation of the enzyme from RNA templates. The elongation rates of
the two enzymes are similar. Finally, a highly distinct property of the
R2 RT, compared with retroviral enzymes, is its ability to displace RNA
strands annealed to RNA templates during cDNA synthesis. We suggest
that both the higher processivity and displacement properties of R2 RT
compared with retroviral RT result from the greater affinity of the R2
protein for the RNA template upstream of its active site.
High Processivity of the Reverse Transcriptase from a Non-long
Terminal Repeat Retrotransposon*
*
This work was supported by National Institutes of Health
Grant GM42790 (to T. H. E.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 585-275-7247;
Fax: 585-275-2070; E-mail: eick@mail.rochester.edu.
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