A directed approach to improving the solubility of Moloney murine leukemia virus reverse transcriptase

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One of the difficulties that can impede structural work on a molecule of interest is limited solubility. Although functionally similar to the human immunodeficiency virus type-1 reverse transcriptase (HIV-1 RT), the Moloney murine leukemia virus reverse transcriptase (MMLV RT) differs both in architecture and solubility properties. Reverse transcriptase is an essential retroviral enzyme that replicates the single-stranded RNA genome of the retrovirus producing a double-stranded DNA copy, which is subsequently integrated into the host's genome. We have introduced a single amino acid substitution in the connection domain of an N-terminally truncated MMLV RT (L435K) that significantly improves the solubility of the enzyme eliminating the need for nonionic detergents in buffering storage solutions. The substituted enzyme retains near wild-type polymerase activity. An important consequence of the improved solubility of the L435K MMLV RT has been the ability to obtain diffraction quality crystals.

Original languageEnglish (US)
Pages (from-to)1936-1941
Number of pages6
JournalProtein Science
Issue number10
StatePublished - Oct 10 2001



  • Crystallization
  • Moloney murine leukemia virus
  • Mutant
  • Reverse transcriptase
  • Solubility

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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