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J. Biol. Chem., Vol. 276, Issue 45, 42543-42548, November 9, 2001
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From the Department of Chemistry, Loyola University Chicago,
Chicago, Illinois 60626
Ribonuclease P (RNase P) catalyzes the 5'-end
maturation of transfer RNA molecules. Recent evidence suggests that the
eukaryotic protein subunits may provide substrate-binding functions
(True, H. L., and Celander, D. W. (1998) J. Biol.
Chem. 273, 7193-7196). We now report that Pop3p, an essential
protein subunit of the holoenzyme in Saccharomyces
cerevisiae, displays novel RNA-binding properties. A recombinant
form of Pop3p (H6Pop3p) displays a 3-fold greater affinity for binding
pre-tRNA substrates relative to tRNA products. The recognition sequence
for the H6Pop3p-substrate interaction in vitro was mapped
to a 39-nucleotide long sequence that extends from position
Novel RNA-binding Properties of Pop3p Support a Role for
Eukaryotic RNase P Protein Subunits in Substrate Recognition*
, and
21 to
+18 surrounding the natural processing site in pre-tRNA substrates.
H6Pop3p binds a variety of RNA molecules with high affinity
(Kd = 16-25 nM) and displays a
preference for single-stranded RNAs. Removal or modification of basic
C-terminal residues attenuates the RNA-binding properties displayed by
the protein specifically for a pre-tRNA substrate. These studies
support the model that eukaryotic RNase P proteins bind simultaneously to the RNA subunit and RNA substrate.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 773-508-3154;
Fax: 773-508-3086; E-mail: dceland@luc.edu.
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