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(Received for publication, July 28, 1995; and in revised form, August 29, 1995) Phospholipid-hydroperoxide glutathione peroxidase (PhGPx) is a
selenoenzyme that reduces hydroperoxides of phospholipid, cholesterol,
and cholesteryl ester. Previous studies suggested that both the
mitochondrial and nonmitochondrial forms of PhGPx are
Volume 270,
Number 45,
Issue of November 10, 1995 pp. 26993-26999
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
cDNA CLONING AND IDENTIFICATION OF MULTIPLE TRANSCRIPTION AND
TRANSLATION START SITES
170 amino
acids long. In this study, we isolated a full-length cDNA clone
encoding rat testis PhGPx. Based on sequence analysis, the cDNA encodes
a protein of 197 amino acids, with translation initiating at
AUG
. The additional 27 amino acids at the N terminus
contain the features of a mitochondrial targeting sequence. In
vitro translation of the full-length PhGPx mRNA initiated
predominantly at AUG
. However, translation initiated at
AUG
when AUG
was deleted. An RNase
protection assay was used to map the 5`-ends of PhGPx mRNAs in rat
tissues. We identified two major windows of transcription initiation
that are tissue-specific. Rat testis predominantly expresses larger
transcripts that encode the 197-amino acid protein containing the
potential mitochondrial targeting signal. The predominant smaller
transcripts in somatic tissues lack AUG
and encode a
170-amino acid protein, which may represent the nonmitochondrial forms
of PhGPx. Our results suggest that the use of alternative transcription
and translation start sites determines the subcellular localization of
PhGPx in different tissues.
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