Amino acid sequence of elongation factor Tu. Sequence of a region containing the thiol group essential for GTP binding

Wade, Michael S.; Laursen, Richard A.; Miller, David L.

doi:10.1016/0014-5793(75)80676-4

Cited by 22 publications

(9 citation statements)

References 9 publications

(6 reference statements)

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“…So far we have detected no differences in the sequences of EF-Tu isolated from these strains. Peptides were generated by cleavage with cyanogen bromide or limited trypsinolysis as described (14)(15)(16)(17); large peptides were further fragmented with trypsin, Staphylococcus aureus protease, or chymotrypsin. Amino acid sequences were determined either by the manual dansyl-Edman procedure (18)(19)(20)(21)(22)(23) or by automated solid-phase Edman degradation (24,25).…”

mentioning

confidence: 99%

Primary structure of elongation factor Tu from Escherichia coli.

Arai¹,

Clark²,

Duffy³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

180

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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 (M, 43,225 for the species bearing COOH-terminal serine). The NHrterminal 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 heterogeneous 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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confidence: 99%

Primary structure of elongation factor Tu from Escherichia coli.

Arai¹,

Clark²,

Duffy³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

180

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“…lo] at the GTP binding site. Although Alakhov et al [9] reported no homology between their peptide and a peptide from EF-Tu [8], a comparison with more recent data [7,1 I] shows clearly that there is homology between the two proteins. Figure 1 shows schematically the two regions being compared.…”

Section: Resultsmentioning

confidence: 78%

“…On the other hand, there must be appreciable differences in structure between the two proteins, since antibodies to EF-G and EF-Tu do not cross react [ 121. The fact that the two cysteines (residue 71 in EF-G and 102 in EF-Tu) reported [8,13,14] to be at the GTPsites are not in homologous regions is not necessarily a problem, because they may simply be in different areas of the GTP binding pockets. There is not yet any evidence that sulfhydryl groups participate in GTP binding, only that they are at or near the binding sites.…”

Section: Resultsmentioning

confidence: 99%

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The evolution of elongation factors Tu and G by gene duplication

Laursen

Duffy

1978

FEBS Letters

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“…In this paper we report that the amino-terminal domain of 112 amino acid residues of LepA shares regions of homology to E. coli translation factors [initiation factor 2, elongation factor Tu, and elongation factor G (IF2, EF-Tu, and EF-G)]. All of these proteins and several other GTP-binding proteins (8) share an adjacent region of similarity, which, in the case of EF-Tu, is known to interact with guanine nucleotides (8)(9)(10) plasmid that overexpresses LepA, has been. described (6).…”

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confidence: 99%