pubmed-article:182140 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C0059037 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
pubmed-article:182140 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
pubmed-article:182140 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:182140 | pubmed:dateCreated | 1976-9-25 | lld:pubmed |
pubmed-article:182140 | pubmed:abstractText | 1. The effect of elongation factor 2 (EF 2) and of adenosine diphosphate-ribosylated elongation factor 2 (ADP-ribosyl-EF 2) on the shift of endogenous peptidyl-tRNA from the A to the P site of rat liver ribosomes (measured by the peptidyl-puromycin reaction) and on the release of deacylated tRNA (measured by aminoacylation) was investigated. 2. Limiting amounts of EF2, pre-bound or added to ribosomes, catalyse the shift of peptidyl-tRNA in the presence of GPT; when the enzyme is added in substrate amounts GMP-P(CH2)P [guanosine (beta, gamma-methylene)triphosphate] can partially replace GTP. ADP-ribosyl-EF 2 has no effect on the shift of peptidyl-tRNA when present in catalytic amounts, but becomes almost as effective as EF 2 when added in substrate amounts together with GTP; GMP-P(CH2)P cannot replace GTP. 3. The release of deacylated tRNA is induced only by substrate amounts of added EF 2 and also occurs in the absence of guanine nucleotides. In this reaction ADP-ribosyl-EF 2 is only 25% as effective as EF 2 in the absence of added nucleotide, but becomes 60-80% as effective in the presence of GTP or GMP-P(CH2)P. 4. The results obtained on protein-synthesizing systems are consistent with the hypothesis that ADP-ribosyl-EF 2 can operate a single round of translocation followed by binding of aminoacyl-tRNA and peptide-bond formation. 5. From the data obtained with the native enzyme it is concluded that the two moments of translocation require different conditions of interaction of EF 2 with ribosomes; it is suggested that the shift of peptidyl-tRNA is catalysed by EF 2 pre-bound to ribosomes, and that the release of tRNA is induced by a second molecule of interacting EF 2. The hydrolysis of GTP would be required for the release of pre-bound EF 2 from ribosomes. 5. The inhibition of the utilization of limiting amounts of EF 2 on ADP-ribosylation is very likely the consequence of a concomitant decrease in the rate of association and dissociation of the enzyme from ribosomes. | lld:pubmed |
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pubmed-article:182140 | pubmed:language | eng | lld:pubmed |
pubmed-article:182140 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:182140 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:182140 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:182140 | pubmed:month | Apr | lld:pubmed |
pubmed-article:182140 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:182140 | pubmed:author | pubmed-author:MontanaroLL | lld:pubmed |
pubmed-article:182140 | pubmed:author | pubmed-author:SpertiSS | lld:pubmed |
pubmed-article:182140 | pubmed:author | pubmed-author:MattioliAA | lld:pubmed |
pubmed-article:182140 | pubmed:author | pubmed-author:TestoniGG | lld:pubmed |
pubmed-article:182140 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:182140 | pubmed:day | 15 | lld:pubmed |
pubmed-article:182140 | pubmed:volume | 156 | lld:pubmed |
pubmed-article:182140 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:182140 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:182140 | pubmed:pagination | 15-23 | lld:pubmed |
pubmed-article:182140 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:182140 | pubmed:year | 1976 | lld:pubmed |
pubmed-article:182140 | pubmed:articleTitle | Effect of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 on translocation. | lld:pubmed |
pubmed-article:182140 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:182140 | pubmed:publicationType | In Vitro | lld:pubmed |
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