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J. Biol. Chem., Vol. 277, Issue 36, 32697-32705, September 6, 2002
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From the Department of Cell Biology and Biochemistry and the
Southwest Cancer Center at University Medical Center, Texas Tech
University Health Sciences Center, Lubbock, Texas 79430
JunD, a member of the Jun family of nuclear
transcription proteins, dimerizes with Fos family members or other Jun
proteins (c-Jun or JunB) to form the activator protein 1 (AP-1)
transcription factor. The junD gene contains no introns and
generates a single mRNA. Here we show that two predominant JunD
isoforms are generated by alternative initiation of translation, a
39-kDa full-length JunD protein (JunD-FL) by initiation at the first
AUG codon downstream of the mRNA 5' cap and a shorter, 34-kDa JunD
protein (
Translational Regulation of the JunD Messenger RNA*
JunD) by initiation at a second in-frame AUG codon. The
JunD mRNA contains a long, G/C-rich 5'-untranslated region that is
predicted to be highly structured and is important for regulating the
ratio of JunD-FL and JunD protein expression. A third functional
out-of-frame AUG directs translation from a short open reading frame
positioned between the JunD-FL and JunD start sites. In addition,
three non-AUG codons also support translation, an ACG codon (in-frame with JunD) and a CUG are positioned in the 5'-untranslated region, and
a CUG codon (also in-frame with JunD) is located downstream of the
short open reading frame . Mutation of these start sites individually
had no affect on JunD protein levels, but mutation of multiple
upstream start sites led to an increase in JunD protein levels,
indicating that these codons can function cumulatively to suppress
JunD translation. Finally, we show that the JunD mRNA does not
possess an internal ribosome entry site and is translated in a
cap-dependent manner.
*
This work was supported by American Heart Association Grant
98BG-381 and Texas Higher Education Coordinating Board Advanced Research Program Grant 010674-0052.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 Cell Biology
and Biochemistry, Texas Tech University Health Sciences Center, 3601 4th St. Lubbock, TX 79430. Tel.: 806-743-1559; Fax: 806-743-2990;
E-mail: curt.pfarr@ttmc.ttuhsc.edu.
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