Volume 272, Number 39,
Issue of September 26, 1997
pp. 24691-24695
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Production of SVP-1/-3/-4 in Guinea Pig Testis
CHARACTERIZATION OF NOVEL TRANSCRIPTS CONTAINING LONG
5
-UNTRANSLATED REGIONS AND MULTIPLE UPSTREAM AUG CODONS
(Received for publication, May 12, 1997, and in revised form, July 28, 1997)
Michael P.
Fautsch
,
Monique M.
Perdok
and
Eric D.
Wieben
From the Department of Biochemistry and Molecular Biology, Mayo
Clinic/Foundation, Rochester, Minnesota 55905
The GP1G gene of the guinea pig codes
for three of the four abundant seminal vesicle secretory proteins
produced in this species. This gene is expressed at highest efficiency
in the seminal vesicle (SV) from a promoter that contains a canonical
TATA box and CCAAT box. However, GP1G gene transcripts and
proteins have also been identified in other tissues. To investigate the
structure of GP1G transcripts produced in the testis,
cDNA clones were isolated by screening a testis library. Three
unique cDNAs (TSM1-3) were isolated. Each of these clones
contained a 3
-untranslated region (UTR) and coding region identical to
that of the seminal vesicle transcript. However, the 5
-UTRs of the
testis transcripts were significantly longer than that found on the SV
mRNA (416-646 nucleotides compared with only 23 nucleotides for
the SV). Each of these alternatively spliced 5
-UTRs incorporated the
SV promoter elements into transcribed sequence, and each contained
multiple upstream AUG codons predicted to abolish translation of the
major open reading frame. Nevertheless, each of the testis transcripts
was capable of directing the synthesis of GP1G-related
proteins in vitro. Analysis of the translation products
suggests that the extended 5
-UTR of the testis transcripts regulate
both the choice of translation start site and the efficiency of
translation in this system. Western blot analysis of testis proteins
revealed that the protein products of GP1G are also
synthesized by the testis in vivo.