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.
Highlights
Human immunodeficiency virus reverse transcriptase is a heterodimeric enzyme comprised of 66- and 51-kDa subunits
Murine leukemia virus reverse transcriptase is functionally active as a monomer
In our effort to identify the region in murine leukemia virus reverse transcriptase (MuLV RT) that obviate the need for dimerization of this enzyme, we compared the primary sequence of MuLV RT with that of human immunodeficiency virus type 1 (HIV-1) RT
Summary
Human immunodeficiency virus reverse transcriptase is a heterodimeric enzyme comprised of 66- and 51-kDa subunits. To ascertain this postulation we constructed a chimeric HIV-1 RT containing two of these motifs and the entire RNase-H domain from MuLV RT. The resulting chimeric HIV-1 RT was found to be a monomeric enzyme with intact polymerase and RNase-H functions.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
