Recent X-ray crystal structure determinations of Moloney murine leukemia virus reverse transcriptase (MoMLV RT) have allowed for more accurate structure/function comparisons to HIV-1 RT than were formerly possible.
2013 Apr 1;41(6):3874-87. doi: 10.1093/nar/gkt053.
https://doi.org/10.1016/j.virusres.2008.01.001. Seven-hundred and sixty eight MMLV RT clones This fragment includes the fingers and palm domains from Moloney murine leukemia virus reverse transcriptase.
Biopolymers. | Substitution of Asp114 or Arg116 in the fingers domain of moloney murine leukemia virus reverse transcriptase affects interactions with the template-primer resulting in decreased processivity. 2014 Apr;21(4):389-96. doi: 10.1038/nsmb.2785. Epub 2014 Feb 15. The eight-site saturation mutage-nesis libraries corresponding to Ala70−Arg469 in the whole MMLV RT (Thr24−Leu671), in each of which 1 out of 50 amino acid residues was replaced with other amino acid residue, were constructed.
J Mol Biol. Ein den Menschen infizierender naher Verwandter von Mo-MLV, das Xenotropic Moloney murine leukemia virus-Related Virus , … Expression of the thermostable Moloney murine leukemia virus reverse transcriptase by silkworm-baculovirus expression system. A 190-base-pair DNA-RNA hybrid containing the Moloney murine leukemia virus origin of plus-strand DNA synthesis was constructed and used as a source of template-primer for the reverse transcriptase in vitro. Protein-DNA interactions, which are nearly identical in each of the three lattices, involve four conserved residues in the fingers domain, Asp114, Arg116, Asn119 and Gly191.
Copyright © 2020 Elsevier B.V. or its licensors or contributors. Get the latest public health information from CDC: https://www.coronavirus.gov. Here, we will review the similarities and differences between MoMLV RT and HIV-1 RT via structural analysis, and propose working models for the MoMLV RT based upon that information. Through site-directed mutagenesis, we have substituted residues that are involved in binding DNA in our crystal structures and have characterized the resulting enzymes. The secondary structures formed in the RNA templates decrease the accessibility of the reverse transcriptase to the RNA templates; it is important to unfold the RNA secondary structure by increasing the reaction temperature to perform the successful transcription. C-terminal tagged MMLVRT showed higher thermostability than that of MMLVRT produced in E. coli.
Protein-nucleic acid interactions and DNA conformation in a complex of human immunodeficiency virus type 1 reverse transcriptase with a double-stranded DNA template-primer. We confirmed that both of the recombinant MMLVRT enzymes have intact DNA polymerase activity. Moloney murine leukemia virus reverse transcriptase (MMLV-RT) 1 is widely used for cDNA preparations and cloning 2 – 5.In a previous report, we showed that MMLV-RT has a strong activity to append 3′-overhangs to double-stranded DNA ends 6.The activity is unique in two respects.
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Proteins. Reverse transcriptase (RT) serves as the replicative polymerase for retroviruses by using RNA and DNA-directed DNA polymerase activities coupled with a ribonuclease H activity to synthesize a double-stranded DNA copy of the single-stranded RNA genome.
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