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  • Title: Xenopus laevis ribosomal protein S11: cloning and sequencing of the cDNA and primary structure of the protein.
    Author: Annesi F, Vespignani I, Amaldi F, Mariottini P.
    Journal: Biochem Biophys Res Commun; 1994 Sep 15; 203(2):768-72. PubMed ID: 8093055.
    Abstract:
    We have cloned a Xenopus laevis cDNA coding for the 40S subunit cytoplasmic ribosomal protein S11. The nucleotide sequence was determined and the derived amino acid sequence reveals that the protein has 158 amino acid residues and a calculated molecular mass of 18,424 Da. Amino acid sequence comparison with the homologous counterparts from very diverse groups of organisms representing animals (human and rat), fungi (yeast) and plants (maize and Arabidopsis thaliana), shows that this protein is very conserved during evolution. Furthermore, ribosomal protein S11 also shares a significant sequence homology to a set of related proteins: plastid ribosomal protein CS17 from different plants, Escherichia coli ribosomal protein S17 and Halobacterium marismortui ribosomal protein S14.
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