A LEUCINE ZIPPER-LIKE MOTIF AND A BASIC REGION-LEUCINE ZIPPER-LIKE ELEMENT IN RAT RIBOSOMAL-PROTEIN L13A - IDENTIFICATION OF THE TUM(-) TRANSPLANTATION ANTIGEN P198

The amino acid sequence of the rat 60 S ribosomal subunit protein L13a was deduced from the sequence of nucleotides in two recombinant cDNAs . Mature ribosomal protein L13a has 202 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and a M(r) of 23, 330. Hybridization of the L13a cDNA to digests of nuclear DNA suggests that there are 9-11 copies of the L13a gene. The mRNA for the protein is similar to 800 nucleotides in length. Rat L13a is related to the S accharomyces cerevisiae ribosomal proteins that have been provisionall y designated rp22 and rp23 and to the eubacterial and archaebacterial family of L13 ribosomal proteins. The mouse tum(-) transplantation ant igen P198 is a mutant of the mouse homolog of rat ribosomal protein L1 3a. Rat ribosomal protein L7 has, at its NH2 terminus, five tandem rep eats of a similar sequence of 12 amino acids (Lin, A., Chan, Y. L., Mc Nally, J., Peleg, D., Meyuhas, O., and Wool, I. G. (1987) J. Biol. Che m. 262, 12665-12671); L13a has, in its carboxyl-terminal region, amino acid sequences with significant identity to L7 repeats 1, 3, and 5. L 13a also has a number of short amino acid sequences that are repeated, a leucine zipper-like moth at its NH2 terminus, and a potential basic region-leucine zipper element in its carboxyl-terminal region.