Document 0002
 DOCN  M95A0002
 TI    Phosphorothioate oligonucleotides block reverse transcription by the
       Rnase H activity associated with the HIV-1 polymerase.
 DT    9510
 AU    Hatta T; Takai K; Yokoyama S; Nakashima H; Yamamoto N; Takaku H;
       Department of Industrial Chemistry, Chiba Institute of; Technology,
       Japan.
 SO    Biochem Biophys Res Commun. 1995 Jun 26;211(3):1041-6. Unique Identifier
       : AIDSLINE MED/95321920
 AB    We demonstrate the degradation of RNA bound to an antisense
       oligonucleotide by a reverse transcriptase enzyme-associated RNase H
       activity. We found that phosphorothioate oligonucleotides inhibit the
       RNase H activity by binding to AMV RT, rather than to the template RNA,
       whereas the RNase H activity of HIV-1 RT is not affected by the
       antisense phosphorothioate oligonucleotide. Selective inhibition of
       HIV-1 gene expression involves the degradation of the template RNA bound
       to the antisense phosphorothioate oligonucleotide by the RNase H
       activity associated with the HIV-1 polymerase.
 DE    Base Sequence  Comparative Study  HIV-1/*ENZYMOLOGY  Molecular Sequence
       Data  Myeloblastosis Virus, Avian/ENZYMOLOGY  Nucleic Acid
       Heteroduplexes/METABOLISM  Oligonucleotides, Antisense/*PHARMACOLOGY
       Reverse Transcriptase/*METABOLISM  Ribonuclease H, Calf
       Thymus/ANTAGONISTS & INHIB/*DRUG EFFECTS  RNA/METABOLISM  Support,
       Non-U.S. Gov't  Thionucleotides/*PHARMACOLOGY  Transcription,
       Genetic/*DRUG EFFECTS  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).