RNase H-mediated cleavage of the RNA strand of the -sssDNA:RNA duplex

Stable Identifier
Reaction [transition]
Homo sapiens
Related Species
Human immunodeficiency virus 1
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As the reverse transcriptase activity of the HIV-1 RT heterodimer catalyzes the synthesis of minus-strand strong stop DNA (-sssDNA), the RNaseH activity of the same RT heterodimer catalyzes the degradation of the complementary viral genomic RNA sequences. Degradation of this RNA is required for the efficient transfer of the -sssDNA to the 5' end of the viral genomic RNA. The RNase H active site is positioned within the HIV-1 RT heterodimer so as to attack the RNA strand of the RNA:DNA duplex at a point 18 bases behind the site of reverse transcription (Furfine and Reardon 1991; Ghosh et al. 1995; Gopalakrishnan et al. 1992; Wohrl and Moelling 1990). The rate of RNase H cleavage is substantially lower than the rate of DNA synthesis, however (Kati et al. 1992), and may further depend on RT stalling and structural features of the viral genomic RNA template. The product of these combined DNA synthesis and RNA degradation events is a DNA strand still duplexed with extended viral genomic RNA fragments.
Literature References
PubMed ID Title Journal Year
7535765 Truncating alpha-helix E' of p66 human immunodeficiency virus reverse transcriptase modulates RNase H function and impairs DNA strand transfer

Le Grice, SF, Benkovic, SJ, Hughes, SH, Howard, KJ, Ghosh, M, Cameron, CE

J Biol Chem 1995
10723025 The HIV-1 reverse transcription (RT) process as target for RT inhibitors

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

Med Res Rev 2000
1702425 Reverse transcriptase.RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities.

Reardon, JE, Furfine, ES

J Biol Chem 1991

Varmus, HE, Hughes, SH, Coffin, JM

Catalyst Activity

RNA-DNA hybrid ribonuclease activity of RTC with minus sssDNA:tRNA primer:RNA template [cytosol]

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