Abstract
Publisher Summary RNA-dependent DNA polymerization (RDDP) activity in the supernatant of cultured cells from an AIDS-afflicted individual was a key in the discovery and characterization of a new pathogenic human immunodeficiency virus (HIV1). The reverse transcriptase (RT) enzyme isolated from the HIV-1 core functionally resembled that of many other retroviruses. Research into HIV RT and reverse transcription has resulted in the biochemical and molecular characterization of several enzymatic processes common to many RNA and DNA polymerases. HIV-1 RT is capable of several enzymatic functions, including RDDP, DNA-dependent DNA polymerization (DDDP), DNA-RNA duplex-dependent ribonuclease activity (RNase HI, and RNA-RNA duplex-dependent ribonuclease activity. It is suggested that in reverse transcription scheme of retroviruses continued polymerization into the PBS at the 3' end of (+) strong-stop DNA requires a switch in RT enzymatic activity from DDDP to RDDP. It has also been reported that HIV-1 RT shows a high mutation rate when compared to other viral RTs.
Published Version
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