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Mol Cell Biol. 1996 Oct;16(10):5645-54.

An unusual mechanism of self-primed reverse transcription requires the RNase H domain of reverse transcriptase to cleave an RNA duplex.

Author information

1
Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA. Henry_Levin@nih.gov

Abstract

The reverse transcription of retroviruses and long terminal repeat-containing retrotransposons requires that tRNA species serve as primers. We recently reported that the long terminal repeat-containing retrotransposon Tf1 is a unique exception in that reverse transcription is independent of tRNA and is instead initiated by a self-priming mechanism. The first 11 bases of the Tf1 transcript fold back and anneal to the primer binding site in a process that results in the priming of minus-strand strong-stop DNA. Data presented here demonstrate that a cleavage occurs between the 11th and 12th bases of the transcript, resulting in the generation of the primer. Mutagenesis experiments presented here indicate that the RNase H domain of the Tf1 reverse transcriptase is required for the cleavage reaction, suggesting that this RNase H may have the novel ability to cleave double-stranded RNA at the end of a duplexed region.

PMID:
8816477
PMCID:
PMC231564
[Indexed for MEDLINE]
Free PMC Article

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