1993
DOI: 10.1006/jmbi.1993.1528
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Structure of a DNA : RNA Hybrid Duplex

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Cited by 250 publications
(240 citation statements)
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“…Although selection and removal of the PPT primer have been accurately recapitulated in biochemical studies with wild type and mutant RT variants (7,20,(23)(24)(25)(26)(27)(28)(29)(30)(31), the structural basis for resistance to internal hydrolysis and specific cleavage at the PPT-U3 junction remains elusive. Analysis of a co-crystal of HIV-1 RT and a PPT-containing RNA/DNA hybrid (4) suggest that the altered groove width observed might not permit correct positioning of the RNA strand in the RNase H catalytic center, a notion put forward by studies of related RNA/DNA hybrids (32)(33)(34)(35)(36)(37)(38). However, our chemical footprinting studies (39) suggest an alternative hypothesis.…”
mentioning
confidence: 83%
“…Although selection and removal of the PPT primer have been accurately recapitulated in biochemical studies with wild type and mutant RT variants (7,20,(23)(24)(25)(26)(27)(28)(29)(30)(31), the structural basis for resistance to internal hydrolysis and specific cleavage at the PPT-U3 junction remains elusive. Analysis of a co-crystal of HIV-1 RT and a PPT-containing RNA/DNA hybrid (4) suggest that the altered groove width observed might not permit correct positioning of the RNA strand in the RNase H catalytic center, a notion put forward by studies of related RNA/DNA hybrids (32)(33)(34)(35)(36)(37)(38). However, our chemical footprinting studies (39) suggest an alternative hypothesis.…”
mentioning
confidence: 83%
“…Initially, the 18-nt duplex region of the tRNA-viral RNA complex adopts an A-form helical geometry, but after incorporation of dNTPs, the primer-template complex becomes a DNA-RNA hybrid and assumes an intermediate conformation in solution (12)(13)(14). X-ray crystallographic structures of RT bound to primer-template complexes (D18 or RNA polypurine tract (PPT) primer annealed to a complementary DNA template) reveal a bend in these complexes of about 40° (15)(16)(17).…”
mentioning
confidence: 99%
“…Finally, Escherichia coli RNase H catalyzes cleavages within the MuLV PPT (9,16,17,19) as well as within the HIV-1 PPT. 3 A second possibility to explain selection of the PPT primer is related to its unique helical structure (12,20) and the shape and width of the major groove, which is wider than that of other RNA-DNA hybrids (20,21). These structural factors could cause binding of RT to the PPT sequence to differ from the way RT binds to other primer-templates (P/T), thereby precluding cleavage within the PPT.…”
mentioning
confidence: 99%