Localization of the Active Site of HIV-1 Reverse Transcriptase-associated RNase H Domain on a DNA Template Using Site-specific Generated Hydroxyl Radicals

Reverse transcriptase (RT)-associated ribonuclease H (RNase H) can cleave both the RNA template of DNA/RNA hybrids as well as double-stranded (ds) RNA. This report shows that human immunodeficiency virus (HIV)-RT can also cleave the template strand of dsDNA when Mg2+ is replaced by Fe2+ in the RNase...

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Veröffentlicht in:	The Journal of biological chemistry 1998-04, Vol.273 (17), p.10139-10146
Hauptverfasser:	Götte, Matthias, Maier, Gottfried, Gross, Hans J., Heumann, Hermann
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites DNA - metabolism DNA Footprinting Ferrous Compounds - metabolism HIV Reverse Transcriptase - metabolism Hydrolysis Hydroxyl Radical - chemistry Magnesium - metabolism Ribonuclease H - metabolism RNA - metabolism Templates, Genetic
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