Nucleic Acids Research, Vol 24, Issue 19 3829-3835, Copyright © 1996 by Oxford University Press
AR Beck, QG Medley, S O'Brien, P Anderson and M Streuli
TIA-1 and TIAR are RNA binding proteins of the RNA recognition motif
(RRM)/ribonucleoprotein (RNP) family that have been implicated as effectors
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
approximately 100 amino acid N-terminal RRM domains and a approximately 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
approximately 1:1, whereas mTIAR isoforms including or lacking the 5'-end
of exon 3 sequences are expressed in a approximately 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.
ARTICLES
Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
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