title: Inhibition of RNase H activity and viral replication by single mutations in the 3' region of Moloney murine leukemia virus reverse transcriptase.
abstract: Selected conserved amino acids in the putative RNase H domain of reverse transcriptase (RT) were modified in a molecularly cloned infectious provirus and in a Moloney murine leukemia virus RT expression vector by site-directed mutagenesis. Substitution of either of two conserved aspartic acid residues in proviral DNA prevented production of infectious particles in transfected NIH 3T3 cells, and the same modifications depressed RT-associated RNase H activity by more than 25-fold with little or no effect on polymerase activity.
authors: Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
authors: R
authors: R
authors: Repaske
authors: J W
authors: JW
authors: Hartley
authors: M F
authors: MF
authors: Kavlick
authors: R R
authors: RR
authors: O'Neill
authors: J B
authors: JB
authors: Austin
mesh_terms: D000595:Amino Acid Sequence; D004252:DNA Mutational Analysis; D004722:Endoribonucleases / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D008979:Moloney murine leukemia virus / Q000201:enzymology / Q000235:genetics*; D012194:RNA-Directed DNA Polymerase / Q000235:genetics* / Q000378:metabolism; D016914:Ribonuclease H; D013329:Structure-Activity Relationship; D014779:Virus Replication
chemical_list: D012194:RNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H