XENOPUS-LAEVIS RIBOSOMAL-PROTEIN S11 - CLONING AND SEQUENCING OF THE CDNA AND PRIMARY STRUCTURE OF THE PROTEIN

We have cloned a Xenopus laevis cDNA coding for the 40S subunit cytopl asmic ribosomal protein S11. The nucleotide sequence was determined an d the derived amino acid sequence reveals that the protein has 158 ami no acid residues and a calculated molecular mass of 18,424 Da. Amino a cid sequence comparison with the homologous counterparts from very div erse groups of organisms representing animals (human and rat), fungi ( yeast) and plants (maize and Arabidopsis thaliana), shows that this pr otein is very conserved during evolution. Furthermore, ribosomal prote in S11 also shares a significant sequence homology to a set of related proteins: plastid ribosomal protein CS17 from different plants, Esche richia coli ribosomal protein S17 and Halobacterium marismortui riboso mal protein S14. (C) 1994 Academic Press, Inc.