title: The primary structure and the functional domains of an elongation factor-1 alpha from Mucor racemosus.
abstract: We have determined the complete nucleotide sequence for TEF-1, one of three genes coding for elongation factor (EF)-1 alpha in Mucor racemosus. The deduced EF-1 alpha protein contains 458 amino acids encoded by two exons. The presence of an intervening sequence located near the 3' end of the gene was predicted by the nucleotide sequence data and confirmed by alkaline S1 nuclease mapping. The amino acid sequence of EF-1 alpha was compared to the published amino acid sequences of EF-1 alpha proteins from Saccharomyces cerevisiae and Artemia salina. These proteins shared nearly 85% homology. A similar comparison to the functionally analogous EF-Tu from Escherichia coli revealed several regions of amino acid homology suggesting that the functional domains are conserved in elongation factors from these diverse organisms. Secondary structure predictions indicated that alpha helix and beta sheet conformations associated with the functional domains in EF-Tu are present in the same relative location in EF-1 alpha from M. racemosus. Through this comparative structural analysis we have predicted the general location of functional domains in EF-1 alpha which interact with GTP and tRNA.
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D004262:DNA Restriction Enzymes; D005796:Genes; D005800:Genes, Fungal; D009089:Mucor / Q000235:genetics* / Q000378:metabolism; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D004262:DNA Restriction Enzymes