Cover: Substitution rates of class-I release factor in eukaryotes. (Upper left) Relative substitution rates of each site were mapped onto human eRF1 tertiary structure (PDB ID: 1DT9) using CN3D version 3.0 (http://www.ncbi.nlm.nih.gov/Structure/CN3D/ cn3d.shtml) [slowly evolving (PUZZLE categories 0 and 1; white), moderately evolving (categories 2-4; orange) and fast evolving (categories 5 and 8; red)]. The positions of the GGQ tripeptide (human eRF1 numbering, 182-184) and the TASNIKS (58-64) heptapeptide on the tertiary structure are indicated. (Upper right) The sites that are significantly diverged in the ciliate eRF1s are highlighted in green. The residue numbers are based on human eRF1 sequence. (Lower left/right) The rear views of the upper left and right structures, respectively. For further details see the paper by Inagaki and Doolittle in this issue: Nucleic Acids Res. (2001) 29, 921-927.
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