Nucleic Acids Research, Vol 26, Issue 11 2565-2572, Copyright © 1998 by Oxford University Press
M Nashimoto, S Geary, M Tamura and R Kaspar
Mammalian tRNA 3' processing endoribonuclease (3' tRNase) can recognize and
cleave any target RNA that forms a precursor tRNA-like complex with another
RNA. Various sets of RNA molecules were tested to identify the smallest RNA
that can direct target RNA cleavage by 3' tRNase. A 3' half tRNAArgwas
cleaved efficiently by 3' tRNase in the presence of small 5' half
tRNAArgvariants, the D stem-loop region of which was partially deleted.
Remarkably, 3' tRNase also cleaved the 3' half tRNAArgin the presence of a
7 nt 5' tRNAArg composed only of the acceptor stem region with a catalytic
efficiency comparable with that of cleavage directed by an intact 5' half
tRNAArg. The catalytic efficiency of cleavage directed by the heptamer
decreased as the stability of the T stem-loop structures of 3' half tRNAArg
variants decreased. No heptamer-directed cleavage of a 3' half tRNAArg
without T stem base pairs was detected. A heptamer also directed cleavage
of an HIV-1 RNA containing a stable hairpin structure. These findings
suggest that in the presence of an RNA heptamer, 3' tRNase can discriminate
and eliminate target RNAs that possess a stable hairpin adjacent to the
heptamer binding sequence from a large complex RNA pool.
ARTICLES
RNA heptamers that direct RNA cleavage by mammalian tRNA 3' processing endoribonuclease
Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA. mnashimoto@chemgate.byu.edu
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