Insight into the Mechanism of the Stabilization of Moloney Murine Leukaemia Virus Reverse Transcriptase by Eliminating RNase H Activity

@article{Mizuno2010InsightIT,
  title={Insight into the Mechanism of the Stabilization of Moloney Murine Leukaemia Virus Reverse Transcriptase by Eliminating RNase H Activity},
  author={Masaki Mizuno and K. Yasukawa and K. Inouye},
  journal={Bioscience, Biotechnology, and Biochemistry},
  year={2010},
  volume={74},
  pages={440 - 442}
}
We explored the mechanism of the stabilization of Moloney murine leukaemia virus reverse transcriptase (MMLV RT) by eliminating RNase H activity. Without the template-primer (T/P) poly(rA)-p(dT)15, the temperature reducing initial reverse-transcription activity by 50% over a 10-min incubation of the RNase H activity-deficient variant D524A was higher by 3.7 °C than that of the wild-type enzyme (WT). In the reverse transcription reaction, the K m values for T/P of WT and D524A were almost the… Expand
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24 Citations
Highly Influential Citations
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Further increase in thermostability of Moloney murine leukemia virus reverse transcriptase by mutational combination
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Increase in thermal stability of Moloney murine leukaemia virus reverse transcriptase by site-directed mutagenesis.
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Preparation and characterization of the RNase H domain of Moloney murine leukemia virus reverse transcriptase.
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Expression of moloney murine leukemia virus reverse transcriptase in a cell-free protein expression system
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Expression of the thermostable Moloney murine leukemia virus reverse transcriptase by silkworm-baculovirus expression system
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Amino acid substitutions away from the RNase H catalytic site increase the thermal stability of Moloney murine leukemia virus reverse transcriptase through RNase H inactivation.
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