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 approximately 800 nucleotides in length. Rat L13a is related to the Saccharomyces cerevisiae ribosomal proteins that have been provisionally designated rp22 and rp23 and to the eubacterial and archaebacterial family of L13 ribosomal proteins. The mouse tum- transplantation antigen P198 is a mutant of the mouse homolog of rat ribosomal protein L13a. Rat ribosomal protein L7 has, at its NH2 terminus, five tandem repeats of a similar sequence of 12 amino acids (Lin, A., Chan, Y. L., McNally, J., Peleg, D., Meyuhas, O., and Wool, I. G. (1987) J. Biol. Chem. 262, 12665-12671); L13a has, in its carboxyl-terminal region, amino acid sequences with significant identity to L7 repeats 1, 3, and 5. L13a also has a number of short amino acid sequences that are repeated, a leucine zipper-like motif at its NH2 terminus, and a potential basic region-leucine zipper element in its carboxyl-terminal region.