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Literature summary for 3.1.26.13 extracted from

  • Talele, T.; Upadhyay, A.; Pandey, V.
    Influence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domains (2009), Virol. J., 6, 159-170.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain Moloney murine leukemia virus
additional information construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ may substitute for Mn2+ Moloney murine leukemia virus
Mg2+ prefered over Mn2+ Human immunodeficiency virus 1
Mn2+ may partially substitute for Mg2+ Human immunodeficiency virus 1
Mn2+ prefered over Mg2+ Moloney murine leukemia virus

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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Moloney murine leukemia virus
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