The mouse S‐antigen gene
- 1 August 1991
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 200 (1) , 95-101
- https://doi.org/10.1111/j.1432-1033.1991.tb21053.x
Abstract
We have characterized a gene for mouse S-antigen and compared its sequence with that of corresponding human and two recently published Drosophila S-antigen genes. The mouse S-antigen gene was approximately 50 kbp in length and consisted of 16 exons and 15 introns. The length of most exons was less than 100 bp and the smallest one was only 10 bp. In contrast, the length of most introns was larger than 2 kbp and the gene consisted of 97% intron and 3% exon. Both splice sites for donor and accepter were in good agreement with the GT/AG rule. S-antigen genes in human and mouse were highly conserved. In contrast, genes for the Drosophila 49-kDa arrestin homolog and arrestin consist of three introns and four exons and two introns and three exons, respectively. The 5'-flanking region of the mouse S-antigen gene, approximately 1.0 kbp long, had no regulatory elements for transcription such as the TATA, CAAT and GC boxes, while a Drosophila arrestin gene has TATA and CAAT boxes. Interestingly, the 5'-flanking region of the mouse gene had promoter activity in an in vitro transcription assay using a nuclear extract of rat brain. A major transcription start site was found at 387 bp upstream from the translation start codon ATG in mouse. From our results, and those of others, we suggest that the S-antigen gene has evolved from a common ancestor gene by either insertion or deletion of introns. Such an alteration of gene structure may have played a role in the evolution of the S-antigen.Keywords
This publication has 39 references indexed in Scilit:
- Binding of GTP to transducin is not inhibited by arrestin and phosphorylated rhodopsinFEBS Letters, 1990
- Rat pineal S‐antigen: Sequence analysis reveals presence of α‐transducin homologous sequenceFEBS Letters, 1989
- Structural analysis of mouse S-antigenGene, 1988
- The sequence of human retinal S‐antigen reveals similarities with α‐transducinFEBS Letters, 1988
- Molecular cloning of the S-antigen cDNA from bovine retinaBiochemical and Biophysical Research Communications, 1987
- A 48 kDa protein arrests cGMP phosphodiesterase activation in retinal rod disk membranesFEBS Letters, 1986
- Blockade of Visual Excitation and Adaptation in Limulus Photoreceptor by GDP-β-SScience, 1986
- Light‐induced binding of 48‐kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsinFEBS Letters, 1984
- Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsinCell, 1983
- Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencingJournal of Molecular Biology, 1980