Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR

被引:81
|
作者
Beck, ARP
Medley, QG
OBrien, S
Anderson, P
Streuli, M
机构
[1] HARVARD UNIV,SCH MED,DEPT PATHOL,BOSTON,MA 02115
[2] HARVARD UNIV,SCH MED,DEPT MED,BOSTON,MA 02115
[3] DANA FARBER CANC INST,DIV TUMOR IMMUNOL,BOSTON,MA 02115
[4] ETH ZENTRUM,BIOCHEM LAB 1,CH-8092 ZURICH,SWITZERLAND
关键词
D O I
10.1093/nar/24.19.3829
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
TIA-1 and TIAR are RNA binding proteins of the RNA recognition motif (RRM)/ribonucleoprotein (RNP) family that have been implicated as effecters of apoptotic cell death, We report the structures of murine TIA-1 and TIAR (mTIA-1 and mTIAR) deduced from cDNA cloning, the mRNA and protein tissue distribution of mTIA-1 and mTIAR, and the exon-intron structures of the mTIA-1 and mTIAR genes. Both mTIA-1 and mTIAR are comprised of three similar to 100 amino acid N-terminal RRM domains and a similar to 90 amino acid C-terminal auxiliary domain, This subfamily of RRM proteins is evolutionarily well conserved; mTIA-1 and mTIAR are 80% similar to each other, and 96 and 99% similar to hTIA-1 and hTIAR, respectively, The overall exon-intron structures of the mTIA-1 and mTIAR genes are also similar to each other, as well as to the human TIA-1 gene structure, While Northern blot analysis reveals that mTIA-1 and mTIAR mRNAs have a broad tissue distribution, mTIA-1 and mTIAR proteins are predominantly expressed in brain, testis and spleen, At least two isoforms of both mTIA-1 and mTIAR are generated by alternative splicing, Murine TIA-1 isoforms including or lacking the exon 5 encoded sequences are expressed at a ratio of similar to 1:1, whereas mTIAR isoforms including or lacking the 5'-end of exon 3 sequences are expressed in a similar to 1:6 ratio, Molecular characterization of murine TIA-1 and TIAR RNA binding proteins provides the basis for a genetic analysis of the functional roles of these proteins during mammalian development.
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页码:3829 / 3835
页数:7
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