Protein Variants | Comment | Organism |
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D524N | loss of catalytic activity. Construction of vectors encapsidated in virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase. There is a steady decline in direct repeat deletion frequency that correlates with decreases in functional RNase H, with greater than fourfold decreases in repeat deletion frequency observed when 95% of virion reverse transcriptase is RNase H defective | Moloney murine leukemia virus |
Organism | UniProt | Comment | Textmining |
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Moloney murine leukemia virus | - |
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General Information | Comment | Organism |
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physiological function | increasing the stoichiometry of RNase H relative to the amount of functional DNA polymerase by virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase, has minimal effects on direct repeat deletion frequency. DNA synthesis is error prone when directed principally by RNase H mutant reverse transcriptase, suggesting a role for RNase H catalytic integrity in the fidelity of intracellular reverse transcription | Moloney murine leukemia virus |