Deoxynucleoside triphosphate incorporation mechanism of foamy virus (FV) reverse transcriptase: implications for cell tropism of FV.
Here, we investigated the pre-steady-state deoxynucleoside triphosphate (dNTP) incorporation kinetics of primate foamy virus (PFV) reverse transcriptase (RT) in comparison with those of HIV-1 and MuLV RTs. PFV RT displayed a drastic reduction in primer extension at low dNTP concentrations where HIV-1 RT remains highly active, indicating a low dNTP binding affinity in the case of PFV RT. Indeed, kinetic analysis showed that, as observed with MuLV RT, PFV RT exhibits approximately 10 to 80 times lower dNTP binding affinity than HIV-1 RT. These three RTs, however, show similar catalytic activities. In conclusion, PFV RT displays mechanistic distinctions in comparison to HIV-1 RT and shares close similarity to MuLV RT.
Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, NY 14642, USA.
Jose
J
Santos-Velazquez
Baek
B
Kim
D001665:Binding Sites; D017931:DNA Primers / Q000737:chemistry; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D015497:HIV-1 / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D008264:Macrophages / Q000201:enzymology; D008938:Mitosis; D008979:Moloney murine leukemia virus / Q000201:enzymology; D009154:Mutation; D009711:Nucleotides / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D016092:Spumavirus / Q000201:enzymology*
D017931:DNA Primers; D009711:Nucleotides; D012194:RNA-Directed DNA Polymerase; D004259:DNA-Directed DNA Polymerase