Document 0047
 DOCN  M9590047
 TI    Cleavage of the HIV replication primer tRNALys,3 in human cells
       expressing bacterial anticodon nuclease.
 DT    9509
 AU    Shterman N; Elroy-Stein O; Morad I; Amitsur M; Kaufmann G; Department of
       Biochemistry, Tel Aviv University, Israel.
 SO    Nucleic Acids Res. 1995 May 25;23(10):1744-9. Unique Identifier :
       AIDSLINE MED/95303607
 AB    Anticodon nuclease is a bacterial restriction enzyme directed against
       tRNA(Lys). We report that anticodon nuclease also cleaves mammalian
       tRNA(Lys) molecules, with preference and site specificity shown towards
       the natural substrate. Expression of the anticodon nuclease core
       polypeptide PrrC in HeLa cells from a recombinant vaccinia virus
       elicited cleavage of intracellular tRNA(Lys),3. The data justify an
       inquiry into the possible application of anticodon nuclease as an
       inhibitor of tRNA(Lys),3-primed HIV replication. They also indicate that
       the anticodon region of tRNA(Lys) is a substrate recognition site and
       suggest that PrrC harbors the enzymatic activity.
 DE    Animal  Bacterial Proteins/BIOSYNTHESIS/*METABOLISM  Base Sequence
       Comparative Study  Escherichia coli/*METABOLISM  Hela Cells  Human
       HIV/*GENETICS/*PHYSIOLOGY  Mammals  Molecular Sequence Data  Nucleic
       Acid Conformation  Recombinant Proteins/BIOSYNTHESIS/METABOLISM
       Ribonucleases/BIOSYNTHESIS/*METABOLISM  RNA, Transfer,
       Lys/CHEMISTRY/*METABOLISM  Sequence Homology, Nucleic Acid  Substrate
       Specificity  Support, Non-U.S. Gov't  Transfection  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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