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Nucleotide Sequence of a cDNA Encoding an Elongation Factor (EF-1[infinity symbol]) from Barley Primary Leaf

The eukaryotic elongation factor (EF-la) functions in protein synthesis by promoting the GTP-dependent binding of aminoacyl tRNA to ribosomes (Miller and Weissbach, 1977). EF-la is an example of a protein that is directly required for the synthesis of a11 cellular proteins and appears to be also required for cell viability (Cottrella et al., 1985). Genes for EF-la have been isolated from a number of plants including Arabidopsis thaliana (Axelos et al., 1989), tomato (Pokalsky et al., 1989), and Glycine max (Aguilar et al., 1991). The barley (Hordeum vulgare L.) EF-la cDNA described here showed 88.7% homology with Arabidopsis, 86.7 with tomato, and 86% with G. max. A cDNA library of poly(A)+ RNA from barley primary leaves was constructed (Chang, 1993). A 1590-bp cDNA was identified and subcloned into pUC19. The dideoxy chaintennination method was utilized to sequence this cDNA insert (National Bioscience Inc., Plymouth, MN). Characteristics of the barley EF-la factor are described in Table I. A previous comparison was made between the Escherichia coli elongation factors EF-G and EF-Tu with the LepA gene product (March and Inouye, 1985). We have extended the comparison by including the deduced amino acid sequences for wheat (Metz et al., 1992) and barley elongation factors. The phosphate-binding loop found in most guanine nucleotide-binding proteins is found at positions 8 to 15 in the barley amino acid sequence and at positions 15 to 22 in the wheat sequence (Saraste et al., 1990). Two other conserved regions included region 1, Arg-Gly-Ile-Thr-Ile, and region 2, Pro-Gly-His. Both regions are maintained unmodified in the bacteria and cereals sequences.