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

Stable Identifier
R-HSA-173769
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Human immunodeficiency virus 1
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
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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
1370087 Incomplete removal of the RNA primer for minus-strand DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase

Pullen, KA, Ishimoto, LK, Champoux, JJ

J Virol 1992
10723025 The HIV-1 reverse transcription (RT) process as target for RT inhibitors

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

Med Res Rev 2000
  Retroviruses

Coffin, JM, Hughes, SH, Varmus, HE

  1997
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
RNA-DNA hybrid ribonuclease activity of RTC with extending second-strand DNA [cytosol]
Physical Entity
Activity
Disease
Name Identifier Synonyms
Human immunodeficiency virus infectious disease 526 HIV infection
Authored
Reviewed
Created
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