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Details on Person RNase H catalyzes the precise cleavage of the bonds linking ...

Class:IdSummation:177430
_displayNameRNase H catalyzes the precise cleavage of the bonds linking ...
_timestamp2006-10-17 19:40:09
created[InstanceEdit:177417] D'Eustachio, P, 2006-03-30 15:26:43
literatureReference[LiteratureReference:177456] Incomplete removal of the RNA primer for minus-strand DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase
[LiteratureReference:182836] 'Binding, bending and bonding': polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus
modified[InstanceEdit:182820] Gopinathrao, G, 2006-07-19 16:21:19
[InstanceEdit:183136] D'Eustachio, P, 2006-07-21 15:54:07
[InstanceEdit:188333] Gopinathrao, G, 2006-10-06 22:15:12
[InstanceEdit:188558] D'Eustachio, P, 2006-10-17 19:40:04
textRNase 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).

(summation)[Reaction:173769] RNase H-mediated digestion of tRNA, 3'PPT and cPPT RNA primers [Homo sapiens]
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