山梨医科大学雑誌　第7巻4号　151-156(1992)

Domain and Modular Structure of Acidic Ribosomal Proteins of
the Yeast Saccharomyces cerevisiae

Kunio TRURUGI

Abstract: The acidic ribosomal protein family of the yeast Saccharomyces cerevisiae consists of five members, one 38-kDa and four 13-kDa proteins, which share homologous carboxyl-terminal sequences of about 50 amino acid residues in length. I showed that the 38-kDa protein, named A0,and the 13-kDa porteins are composed of five and three domains, respectively, based on characteristics in the primary sequences, of which domains 4 and 5 of A0 are homologous or identical to domains 2 and 3 of 13-kDa proteins. Both domain 3 of A0, containing the leucine zipper, and domain 2, containing three pairs of evolutionarily conserved phenylalanine residues, are composed of three repeated segments, although homologies among the segments are lower than those of domain 3. Although the sequences of domain 1 of 13-kDa proteins show little similarity to that of domain 2 of A0, they are also composed of modular structures having a bilateral hydrophobic zipper. Thus, it is likely that the 13-kDa proteins and the carboxyl half of the 38-kDa protein have diverged from a common ancient gene by gene duplication. Further, an evolutionary analysis of the nucleotide sequences suggests that the similarity, even the identity, of domain 3 (or domain 5 of A0), in amino acid sequences have been conserved independently after divergence. However, the identity in the nucleotide sequences of the carboxyl-terminal domain 3 of the two 13-kDa protein, L44 and A2, presents the possibility of inter-gene conversion.

Key words: Yeast, Ribosome, Acidic proteins, Domain structure, Gene duplication




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