The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites.
The primary structure of the alpha subunit of elongation factor 1 (EF-1 alpha) from human MOLT 4 cells was determined by cDNA sequencing. The data show that the conservation of the amino acid sequence is more than 80% when compared with yeast and Artemia EF-1 alpha. An inventory of amino acid sequences around the guanine-nucleotide-binding site in elongation factor Tu from Escherichia coli and homologous amino acid sequences in G proteins, initiation and elongation factors and proteins from the RAS family shows two regions containing conserved sequence elements. Region I has the sequence apolar-Xaa-Xaa-Xaa-Gly-Xaa-Xaa-Yaa-Xaa-Gly-LYs-Thr(Ser)- -Xaa-Xaa-Xaa-Xaa-X-apolar. Except for RAS proteins, Yaa is always an acidic amino acid residue. Region II is characterized by the invariant sequence apolar-apolar-Xaa-Xaa-Asn-Lys-Xaa-Asp. In order to facilitate sequence comparison we have used a graphic display, which is based on the hydrophilicity values of individual amino acids in a sequence.
D000595:Amino Acid Sequence; D000818:Animals; D001156:Artemia; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004247:DNA; D006150:Guanine Nucleotides / Q000378:metabolism*; D006801:Humans; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000378:metabolism; D012441:Saccharomyces cerevisiae
D006150:Guanine Nucleotides; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D004247:DNA