Primary structure of elongation factor Tu from Escherichia coli.

Arai, Kohei; Clark, Brian F. C.; Duffy, Lawrence K.; Jones, Michael D.; Kaziro, Yoshito; Laursen, Richard A.; L’Italien, James; Miller, David L.; Nagarkatti, S; Nakamura, Shun; Nielsen, Karen Margrethe; Petersen, Torben E.; Takahashi, Kenji; Wade, Michael S.

doi:10.1073/pnas.77.3.1326

Cited by 180 publications

(64 citation statements)

References 48 publications

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“…A preliminary account of the Si nuclease analysis was given (4). We show in this report that Eco-N codes for a protein of 408 aminoacids which is highly homologous to the E. coli EF-Tu protein (5,6). The …”

Section: Introductionmentioning

confidence: 99%

Nucleotide sequence of aEuglena gracilischloroplast genome region coding for the elongation factor Tu; evidence for a spliced mRNA

1983

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Section: Introductionmentioning

confidence: 99%

Nucleotide sequence of aEuglena gracilischloroplast genome region coding for the elongation factor Tu; evidence for a spliced mRNA

1983

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“…The primary structure of E. coli EF-Tu has been determined on the basis of its DNA [86] and protein sequence [87] and considerable progress has been made in the elucidation of the tertiary structure of the EF-Tu -GDP complex by means of Xray crystallography [88,89]. The three-dimensional structures of various tRNAs have been resolved [90] and besides tRNA .…”

Section: Discussionmentioning

confidence: 99%

Structural features in aminoacyl‐tRNAs required for recognition by elongation factor Tu

Faulhammer¹,

Joshi²

1987

FEBS Letters

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In bacterial polypeptide synthesis aminoacyl-tRNA (aa-tRNA) bound to elongation factor Tu (EF-Tu) and GTP is part of a crucial intermediate ribonucleoprotein complex involved in the decoding of messenger RNA. The conformation and topology as well as the affinity of the macromolecules in this ternary aatRNA-EF-TuGTP complex are of fundamental importance for the nature of the interaction of the complex with the ribosome. The structural elements of aa-tRNA required for interaction with EF-Tu and GTP and the resulting functional implications are presented here.

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“…The segment lengths employed were 10, 20,25,40,80,87 and 174, and for each run 100 randomisations of the sequence were performed. The 87-residue strings were all compared with each other.…”

Section: Search Programmentioning

confidence: 99%

“…The following proteins were compared with protein Sl: all 53 ribosomal proteins derived from the E. coli ribosome (for references see [l If, except for S2 (121, L2 1133[l If, except for S2 (121, L2 , L9 1141 and S14 1161); proteins associated with the ribosome, namely NSl and NS2 [17] as well as the factors, EC-IF-l [18], EC-IF-3 1191 and EC-EF-Tu [20]; all protein sequences contained in [9].…”

Section: Proteins Used For the Comparison 22 Statistical Analysismentioning

confidence: 99%

Multiple internal repeats within protein S1 from the Escherichia coli ribosome

1983

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The complete sequence determination of protein S 1, the largest protein from the Escherichia coli ribosome, revealed that it is composed of repeated internal duplications, mainly at the central region of the molecule which contains the mRNA-binding domain [Eur. J. Biochem. (1982) 123, 37-531. With the aid of computer programs the statistical significance of the internal repeats in Sl was proven. Auto-comparison of the Sl-sequence showed that it is composed of 87-residue strings with 44-residue subunits: 3 strings (residues 189-447) are highly related; 3 strings (residues 13-188 and 448-533) are less but significantly related. Statistical analysis revealed a more distant relatedness for the 44-residue subunits than for the 87-residue strings. Protein Sl was compared to all other E. coli ribosomal proteins and to the 1100 primary structures listed in the last Atlas of Protein Sequence and Structure (1978) showing parts of Sl distantly related with parts of several ribosomal proteins. However, distinct homologies between protein Sl and the other ribosomal proteins can be ruled out. The strongest repeats within the Sl sequence were mainly found corresponding to the mRNA-binding domain. Distantly related partial sequences were also found with ribosome-associated and nucleotide-binding proteins, with some enzymes, with several peptide hormones and with contractile proteins. Ribosomal protein SI

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Primary structure of elongation factor Tu from Escherichia coli.

Cited by 180 publications

References 48 publications

Nucleotide sequence of aEuglena gracilischloroplast genome region coding for the elongation factor Tu; evidence for a spliced mRNA

Nucleotide sequence of aEuglena gracilischloroplast genome region coding for the elongation factor Tu; evidence for a spliced mRNA

Structural features in aminoacyl‐tRNAs required for recognition by elongation factor Tu

Multiple internal repeats within protein S1 from the Escherichia coli ribosome

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