J. Biochem, 1995, Vol. 118, No. 2 380-389
© 1995 Japanese Biochemical Society
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Genomic Organization and Isoforms of the Mouse ELP Gene1
*Department of Molecular Pathology, Research Institute for Radiation Biology and Medicine, Hiroshima University 1-2-3 Kasumi, Minami-ku, Hiroshima 734
Department of Biochemistry and Biophysics, Research Institute for Radiation Biology and Medicine, Hiroshima University 1-2-3 Kasumi, Minami-ku, Hiroshima 734
2 Present address: Laboratory of Biochemistry, National Cancer Institute, NIH, Bethesda, MD 20892, USA
3 To whom correspondence should be addressed.
Analysis was made on the genomic structure, functions, and expression of the mouse ELP gene, which codes for the embryonal long terminal repeat binding protein. Extensive screening of the cDNA library of embryonal carcinoma cells (EC cells) identified four isoforms of ELP: (ELP1the original ELP isolate), ELP2, ELP3, and Ad4BP/SF1. Analysis of the genomic sequences revealed that these ELP isoforms were generated by alternative promoter usage and differential splicing. The mRNAs of isforms initiated at four transcription start sites distributed on three exons. Sequence analysis of the four isoforms identified three polypeptides. The Nterminal portion of ELP1 and ELP2 was longer than ELP3, and Ad4BP/SF1 by 77 aa. The DNA-binding domain and region II were shared by all four isoforms. The C-terminal portion shared by ELP2, ELP3, and Ad4BP/SF1 was 131 aa in length, and that specific to ELP1 was 57 aa in length. The ELP3 and Ad4BP/SF1 isoforms were identical for the coding sequence, but the two differed at the 5' noncoding region. Region II and III domains of nuclear receptors were thought to be involved in ligandbinding and transcriptional activation. ELP1, which lacked region III, functioned as a repressor. The isoforms carrying intact region II and region III functioned as transactivators. Expression of the four isoforms was studied in mouse tissues and in tissue culture cells by quantitative reverse transcriptase-polymerase chain reaction (RT-PCR) analysis. Complex patterns of expression of these isoforms were observed in varioustissues. All four ELP isoforms were expressed only in EC cells.
1This work was supported by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan. The nucleotide sequence data reported in this paper will appear in the GSDB, DDBJ, EMBL, and NCBI nucleotide sequence databases with accession numbers of D49681-D49683.
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