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. 1980 Mar;77(3):1326–1330. doi: 10.1073/pnas.77.3.1326

Primary structure of elongation factor Tu from Escherichia coli.

K Arai, B F Clark, L Duffy, M D Jones, Y Kaziro, R A Laursen, J L'Italien, D L Miller, S Nagarkatti, S Nakamura, K M Nielsen, T E Petersen, K Takahashi, M Wade
PMCID: PMC348487  PMID: 6990408

Abstract

The amino acid sequence of elongation factor Tu (EF-Tu) from Escherichia coli has been determined. EF-Tu is a single-chain polypeptide composed of 393 amino acids (Mr 43,225 for the species bearing COOH-terminal serine). The NH2-terminal serine is acetylated, and lysine-56 is partially methylated. The sites of facile tryptic cleavage are at arginines 44 and 58 and at lysine-263. The cysteinyl residues associated with aminoacyl-tRNA and guanosine nucleotide binding activities are residues 81 and 137, respectively. The COOH-terminal amino acid is heterogenous in that analyses of the COOH-terminal peptides isolated from different EF-Tu preparations gave position 393 as glycine and serine in ratios (Gly/Ser) ranging from about 0.7 to 3.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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