An enzymatically active chimeric HIV-1 reverse transcriptase (RT) with the RNase-H domain of murine leukemia virus RT exists as a monomer.

The Journal of Biological Chemistry
H S MisraV N Pandey

Abstract

The existence of retroviral reverse transcriptases as monomers or dimers is rather intriguing. A classical example of the former is murine leukemia virus reverse transcriptase (MuLV RT), while human immunodeficiency virus type 1 (HIV-1) RT represents the latter. A careful scrutiny of the amino acid sequence alignment of the two enzymes pinpoints the region tentatively responsible for this phenomenon. We report here the construction of a chimeric enzyme containing the first 425 amino acid residues from the N-terminal domain of HIV-1 RT and 200 amino acid residues from the C-terminal domain of MuLV RT. The chimeric enzyme exists as a monomer with intact DNA polymerase and RNase-H functions.

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Citations

Mar 21, 2000·Medicinal Research Reviews·H JonckheereE De Clercq
Nov 25, 2005·The Journal of Biological Chemistry·Sharon J SchultzJames J Champoux
Oct 17, 2008·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Swathi Kota, Hari S Misra
Sep 21, 2001·Nucleosides, Nucleotides & Nucleic Acids·E LobatónM J Camarasa

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