Nucleotide sequence analysis of the approximately 35-kb segment containing interferon-gamma-inducible mouse proteasome activator genes.
The proteasome activator PA28 is an interferon-gamma-inducible complex made up of two related subunits, named PA28 alpha and PA28 beta, with approximately 50% amino acid sequence identity. Accumulated evidence indicates that binding of this complex to the 20S proteasome enhances the generation of class I-binding peptides. Previously, we showed that the genes coding for PA28 alpha and PA28 beta, designated Psme1 and Psme2, respectively, are located approximately 6 kb apart with their 3' ends pointing toward each other on mouse Chromosome 14. In the present study, we sequenced the regions adjacent to Psme1 and Psme2. In a contiguous stretch of approximately 35 kb, we identified six genes arranged in the following order: Cg10671-like (a gene similar to Drosophila CG10671)-Psme1-Cgi112 (a ubiquitously expressed gene with no known function)-Psme2-Flj10111 (a gene coding for a protein with two RING finger domains)-Isgf3g (an interferon-gamma-inducible gene coding for an interferon-dependent, positive-acting transcription factor 3 gamma). Interestingly, the 3' untranslated region of Psme1 overlaps with that of Cgi112 by 7 bp. Database analysis indicates that the corresponding human genes also overlap by up to 7 bp in their 3' untranslated regions. The 5' end of the mouse, but not the human, gene coding for PA28 beta undergoes alternative splicing that is predicted to alter the N-terminal amino acid sequence. Comparison of the mouse sequence with a human draft sequence deposited in the NCBI database revealed that the overall organization of the region coding for the interferon-gamma-inducible proteasome activator is conserved between human and mouse.
Yawata
M
M
CREST, Japan Science and Technology Corporation (JST), Hayama 240-0193, Japan. kasahara@soken.ac.jp
Murata
S
S
Tanaka
K
K
Ishigatsubo
Y
Y
Kasahara
M
M
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001324:Autoantigens; D001483:Base Sequence; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D017931:DNA Primers / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics; D004789:Enzyme Activation; D005091:Exons; D006801:Humans; D007371:Interferon-gamma / Q000494:pharmacology*; D051379:Mice; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000378:metabolism*; D009124:Muscle Proteins; D046988:Proteasome Endopeptidase Complex; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D001324:Autoantigens; D017931:DNA Primers; D018076:DNA, Complementary; C099558:Ki antigen; D009097:Multienzyme Complexes; D009124:Muscle Proteins; C085047:PSME1 protein, human; D011506:Proteins; D012333:RNA, Messenger; D007371:Interferon-gamma; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; C486213:Psme1 protein, mouse; C486214:Psme2 protein, mouse