The primary structure of elongation factor from <i>Escherichia coli</i>

Ovchinnikov, Yu.A.; Alakhov, Yu.B.; Bundulis, Yu.P.; Bundule, M.A.; Dovgas, N.V.; Kozlov, V. P.; Motuz, L.P.; Vinokurov, Leonid M.

doi:10.1016/0014-5793(82)80503-6

Cited by 42 publications

(9 citation statements)

References 15 publications

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“…In this communication we report the cloning and initial characterization of the gene encoding the rat mitochondrial elongation factor G (rEF-Gmt). Our findings show that rEF-Gmt is a highly conserved (10,(16)(17)(18) GTP binding protein (18)(19)(20)(21)(22)(23)(24)(25)(26) whose function is restricted to the mitochondrial ribosomes (27)(28)(29)(30). Expression of rEF-G, was detected in all tissues with the highest levels in liver, thymus and brain.…”

Section: Introductionmentioning

confidence: 94%

Identification of the gene encoding the mitochondrial elongation factor G in mammals

et al. 1993

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Protein synthesis in cytosolic and rough endoplasmic reticulum associated ribosomes is directed by factors, many of which have been well characterized. Although these factors have been the subject of intense study, most of the corresponding factors regulating protein synthesis in the mitochondrial ribosomes remain unknown. In this report we present the cloning and initial characterization of the gene encoding the rat mitochondrial elongation factor-G (rEF-Gmt). The rat gene encoding EF-Gmt (rMef-g) maps to rat chromosome 2 and it is expressed in all tissues with highest levels in liver, thymus and brain. Its DNA sequence predicts a 752 amino acid protein exhibiting 72% homology to the yeast Saccharomyces cerevisiae mitochondrial elongation factor-G (YMEF-G), 62% and 61% homology to the Thermus thermophilus and E. coli elongation factor-G (EF-G) respectively and 52% homology to the rat elongation factor-2 (EF-2). The deduced amino acid sequence of EF-G contains characteristic motifs shared by all GTP binding proteins. Therefore, similarly to other elongation factors, the enzymatic function of EF-Gmt is predicted to depend on GTP binding and hydrolysis. EF-Gmt differs from its cytoplasmic homolog, EF-2, in that it contains an aspartic acid residue at amino acid position 621 which corresponds to the EF-2 histidine residue at position 715. Since this histidine residue, following posttranslational modification into diphthamide, appears to be the sole cellular target of diphtheria toxin and Pseudomonas aeruginosa endotoxin A, we conclude that EF-Gmt will not be inactivated by these toxins. The severe effects of these toxins on protein elongation in tissues expressing EF-Gmt suggest that EF-Gmt and EF-2 exhibit nonoverlapping functions. The cloning and characterization of the mammalian mitochondrial elongation factor G will permit us to address its role in the regulation of normal mitochondrial function and in disease states attributed to mitochondrial dysfunction.

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Section: Introductionmentioning

confidence: 94%

Identification of the gene encoding the mitochondrial elongation factor G in mammals

et al. 1993

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“…val-leuvalgiyasncys-leu-alaalaarg-thr-ivalguser-arg-glnala-glnasp-leua, Amons et al (1983); b, Arai et al (1980); c, Ovchinnikov et al (1982);d, Ponstingl et al (1981); e, Krauhs et al (1981); f, Capon et al (1983) and Reddy (1983) for c-has/bas gene product. p21-has ) has glycine at position 122 and p21-kis (Suchida et al, 1982) has, in this region, differences at residues 107 (glu), 121-122 (pro-ser), 126-128 (asp-thr-lys) and 132 (glu).…”

Section: H 80mentioning

confidence: 99%

“…We have therefore compared the known amino acid sequences of six GTP-binding proteins to see if there exist homologous regions which might be tentatively identified as participating in nucleotide binding. The protein sequences examined were of Escherichia coli EF-Tu (Arai et al, 1980), E. coli EF-G (Ovchinnikov et al, 1982), alpha-tubulin , beta-tubulin , p21 (Capon et al, 1983;Reddy, 1983), p21 has , p21 kis (Tsuchida et al, 1982), and IRL Press Limited, Oxford, England. the partial sequence of Artemia salina eEF-Tu (Amons et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21.

Leberman¹,

Egner²

1984

The EMBO Journal

112

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An examination of the available amino acid sequences of GTP‐binding proteins has revealed that each contains a polypeptide essentially homologous for all of them. These sequences for elongation factor‐Tu (EF‐Tu) and the human bladder protein p21 exhibit a singular degree of homology (50%). Chemical and structural evidence indicates that this sequence in EF‐Tu constitutes part of the nucleotide‐binding site. The homologous sequences may therefore contribute to the GTP‐binding sites of the other proteins.

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“…2.5-times larger than EFTu and there are considerable homologies in the Nterminal sequences beween the two [13,14] it may be speculated that EF-G evolved at a later stage than EF-Tu. It is possible that the mechanism of initiation in protein synthesis also developed at a later stage.…”

Section: Discussionmentioning

confidence: 99%

Conformational change of 50 S ribosomes on enzymatic binding of phenylalanyl‐tRNA

Srivastava¹,

Burma²

1985

FEBS Letters

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Tight couple 70 S ribosmes are converted to loose couple ones on enzymatic binding of phenylalanyl-tRNA. Enzymatic binding at 0°C as well as nonenzymatic binding does not lead to any change. Further, no change takes place when the P site is occupied by N-acetylphenylalanyl-tRNA.Loose couple 70 S ribosomes are not affected by either enzymatic or nonenzymatic binding of phenylalany-tRNA. S ribosomeConformationai change Phe-tRNA binding SO S ribosome

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The primary structure of elongation factor from Escherichia coli

Cited by 42 publications

References 15 publications

Identification of the gene encoding the mitochondrial elongation factor G in mammals

Identification of the gene encoding the mitochondrial elongation factor G in mammals

Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21.

Conformational change of 50 S ribosomes on enzymatic binding of phenylalanyl‐tRNA

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