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Identification and characterization of a cDNA encoding ribosomal protein S12 from Xenopus laevis |
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| Authors: | L. T. Seery D. R. Schoenberg M. E. Canning A. S. Whitehead |
| Affiliation: | a Department of Genetics and Biotechnology Institute, Trinity College, Dublin 2, Ireland b Department of Pharmacology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD 20814, USA. Tel. (1-30 |
| Abstract: | The complete nucleotide (nt) sequence of the cDNA clone XL-S12, encoding a Xenopus laevis (XI) homologue of the mammalian ribosomal protein S12, has been determined. The sequence predicts a XI S12 protein of 132 amino acids (aa) with a molecular mass of 14.7 kDa. XI S12 shares 95 and 97% aa sequence identity with the human and murine S12 proteins, respectively. Analysis of nt substitution patterns and rates indicates that S12 is a very highly constrained protein, evolving at an estimated rate of only 0.03 x 10˜9 non-synonymous (protein-altering) substitutions per site per year. |
| Keywords: | Phylogeny nucleotide sequence and substitution rate evolution rate |
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