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J. Biol. Chem., Vol. 275, Issue 35, 26710-26719, September 1, 2000
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From the Neurospora crassa arg-2 mRNA
contains an evolutionarily conserved upstream open reading frame (uORF)
encoding the Arg attenuator peptide (AAP) that confers negative
translational regulation in response to Arg. We examined the regulatory
role of the AAP and the RNA encoding it using an N. crassa
cell-free translation system. AAPs encoded by uORFs in four fungal
mRNAs each conferred negative regulation in response to Arg by
causing ribosome stalling at the uORF termination codon. Deleting the
AAP non-conserved N terminus did not impair regulation, but deletions
extending into the conserved region eliminated it. Introducing many
silent mutations into a functional AAP coding region did not eliminate
regulation, but a single additional nucleotide change altering the
conserved AAP sequence abolished regulation. Therefore, the conserved
peptide sequence, but not the mRNA sequence, appeared responsible
for regulation. AAP extension at its C terminus resulted in
Arg-mediated ribosomal stalling during translational elongation within
the extended region and during termination. Comparison of Arg-mediated stalling at a rare or common codon revealed more stalling at the rare
codon. These data indicate that the highly evolutionarily conserved
peptide core functions within the ribosome to cause stalling;
translational events at a potential stall site can influence the extent
of stalling there.
Evolutionarily Conserved Features of the Arginine Attenuator
Peptide Provide the Necessary Requirements for Its Function in
Translational Regulation*
,§, and¶
Department of Biochemistry and Molecular
Biology, Oregon Graduate Institute of Science & Technology, Beaverton,
Oregon 97006-8921 and the ¶ Department of Molecular Microbiology
and Immunology, Oregon Health Sciences University,
Portland, Oregon 97201-3098
*
This work was supported by National Institutes of Health
Grant GM47498.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: Dept. of
Biochemistry and Molecular Biology, Oregon Graduate Inst. of Science & Technology, 20000 N.W. Walker Rd., Beaverton, OR 97006-8921. Tel.:
503-748-1487; Fax: 503-748-1464; E-mail:
msachs@bmb.ogi.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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