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150-kb Region Containing the
- and ß-Subunit Genes1 ,2
,
,§
*
Department of Biochemistry, Hokkaido University School of Medicine, Sapporo 060, Japan;
Biomedical R&D Department, Sumitomo Electric Industries, Yokohama 244, Japan;
CREST (Core Research for Evolutional Science and Technology), Japan Science and Technology Corporation, Japan;
§
Tokyo Metropolitan Institute of Medical Science, Tokyo 113, Japan; and
¶
Laboratory of Animal Genetics, Nagoya University School of Agricultural Sciences, Nagoya 464-01, Japan
The proteasome is a multisubunit protease responsible for the
generation of peptides loaded onto MHC class I molecules. Recent
evidence indicates that binding of an IFN-
-inducible PA28 activator
complex to the 20S proteasome enhances the generation of class I
binding peptides. The
- and ß-subunits, which constitute the PA28
activator complex in the form of an (
ß)3
heterohexamer, show significant amino acid sequence similarity to a
protein, designated Ki or the
-subunit, that is capable of binding
to the 20S proteasome. In this study, we describe the complete
nucleotide sequences of the mouse genes, Psme1,
Psme2, and Psme3, coding for the
-, ß-,
and
-subunits, respectively. The overall exon-intron organizations
of the three Psme genes are virtually identical, thus
providing evidence that they are descended from a single ancestral
gene. The promoter regions of the Psme1 and
Psme2 genes contain sequence motifs that qualify as
IFN-stimulated response elements, consistent with the observation that
their expression is induced strongly by IFN-
. The Psme1
and Psme2 genes are located
6 kb apart with their
3'-ends pointing toward each other on bands C2 to D1 of mouse
chromosome 14, supporting the idea that they emerged by tandem
duplication.
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