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(Received for publication, July 9, 1996)
From the S-Adenosylmethionine decarboxylase
(AdoMetDC) is a key enzyme in the pathway of polyamine biosynthesis.
The cellular levels of the polyamines specifically regulate AdoMetDC
translation through the 5
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29576-29582
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Department of Biochemistry, Box 357350, University of Washington, Seattle, Washington 98195 and the
§ Departments of Cellular and Molecular Physiology and
Pharmacology, Milton S. Hershey Medical Center, Pennsylvania State
University College of Medicine, Hershey, Pennsylvania 17033
-leader of the mRNA, which contains a
small upstream open reading frame (uORF) 14 nucleotides from the cap.
Mutating the initiation codon of the uORF, which encodes a peptide
product with the sequence MAGDIS, abolished regulation. In addition,
the uORF is sufficient, by itself, to provide polyamine regulation when
inserted into the 5-leader of the human growth hormone mRNA. Changing the amino acid sequence at the carboxyl terminus of the peptide product of the uORF abolished polyamine regulation. In contrast, altering the nucleotide sequence of the uORF at degenerate positions, without changing the amino acid sequence of the peptide, did
not affect regulation. Extending the distance between cap and uORF,
thereby changing the rate of initiation at the initiator AUG of the
uORF, did not alter polyamine regulation. When the uORF was extended so
as to overlap, out of frame, the downstream major cistron, polyamine
regulation was abolished. We propose that polyamines do not modulate
the rate of recognition of the uORF but rather regulate interaction of
the peptide product of the uORF with its target.
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