RNase H-mediated digestion of tRNA, 3'PPT and cPPT RNA primers

Stable Identifier
Reaction [transition]
Homo sapiens
Related Species
Human immunodeficiency virus 1
Locations in the PathwayBrowser
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RNase H catalyzes the precise cleavage of the bonds linking the primer tRNA attached to the minus-strand DNA, the 3' PPT RNA primer to the plus-strand strong-stop DNA, and the cPPT primer to the stretch of plus-strand DNA whose synthesis it primed. In each case, precise cleavage near the RNA-DNA junction occurs (Pullen et al. 1992). HIV-1 RT is the only reverse transcriptase that cleaves the tRNA:DNA junction so as to leave a ribo A residue from the tRNA at the 5' end of the minus strand.

While a single RT heterodimer could in principle catalyze DNA synthesis and primer RNA:DNA bond cleavage, evidence from several in vitro systems suggests that separate RT heterodimers are likely to catalyze these two reactions (Rausch and Le Grice 2004).

Literature References
PubMed ID Title Journal Year
10723025 The HIV-1 reverse transcription (RT) process as target for RT inhibitors

De Clercq, E, Anne, J, Jonckheere, H

Med Res Rev 2000
1370087 Incomplete removal of the RNA primer for minus-strand DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase

Ishimoto, LK, Pullen, KA, Champoux, JJ

J Virol 1992

Varmus, HE, Hughes, SH, Coffin, JM

Catalyst Activity

RNA-DNA hybrid ribonuclease activity of RTC with extending second-strand DNA [cytosol]

Name Identifier Synonyms
Human immunodeficiency virus infectious disease DOID:526 HIV infection
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