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J Biol Chem, Vol. 274, Issue 6, 3859-3864, February 5, 1999
From the Pokeweed antiviral protein (PAP), a 29-kDa
ribosome-inactivating protein, catalytically removes an adenine residue
from the conserved
Pokeweed Antiviral Protein Accesses Ribosomes by Binding to
L3
,¶
Biotechnology Center for Agriculture and the
Environment and Department of Plant Pathology, Rutgers University, New
Brunswick, New Jersey 08901-8520 and § Department of
Molecular Genetics and Microbiology and The Cancer Institute of New
Jersey and ¶ Graduate Program in Molecular Biosciences at Rutgers,
University of Medicine and Dentistry of New Jersey,
Piscataway, New Jersey 08854
-sarcin loop of the large rRNA, thereby
preventing the binding of eEF-2·GTP complex during protein
elongation. Because the -sarcin loop has been placed near the
peptidyltransferase center in Escherichia coli ribosomes,
we investigated the effects of alterations at the peptidyltransferase
center on the activity of PAP. We demonstrate here that a chromosomal
mutant of yeast, harboring the mak8-1 allele of
peptidyltransferase-linked ribosomal protein L3 (RPL3), is
resistant to the cytostatic effects of PAP. Unlike wild-type yeast,
ribosomes from mak8-1 cells are not depurinated when PAP
expression is induced in vivo, indicating that wild-type L3
is required for ribosome depurination. Co-immunoprecipitation studies
show that PAP binds directly to L3 or Mak8-1p in vitro but
does not physically interact with ribosome-associated Mak8-1p. L3 is
required for PAP to bind to ribosomes and depurinate the 25 S rRNA,
suggesting that it is located in close proximity to the -sarcin
loop. These results demonstrate for the first time that a ribosomal
protein provides a receptor site for an ribosome-inactivating protein
and allows depurination of the target adenine.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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