Relationship between elongation factor 1- and elongation factor 2-dependent guanosine triphosphatase activities of ribosomes. Inhibition of both activities by ricin
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چکیده
منابع مشابه
Inhibition by aminoacyl transfer ribonucleic acid of elongation factor G-dependent binding of guanosine nucleotide to ribosomes.
Ribosomes complexed with poly(U) and Phe-transfer RNA (tRNA) have been examined for their ability to interact with elongation factor G (EF-G). It is shown that PhetRNA, bound to ribosomes either at 6 mM Mg2+ in the presence of elongation factor Tu and GTP or at 20 rn~ Mg2+ in the absence of these compounds, strongly inhibits (50 to 90%) the binding of EF-G, as measured by the formation of eithe...
متن کاملEffects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens.
Low-temperature-adapted archaea are abundant in the environment, yet little is known about the thermal adaptation of their proteins. We have previously compared elongation factor 2 (EF-2) proteins from Antarctic (Methanococcoides burtonii) and thermophilic (Methanosarcina thermophila) methanogens and found that the M. burtonii EF-2 had greater intrinsic activity at low temperatures and lower th...
متن کاملInhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes.
Elongation factor G (EF G), bound to ribosomes either with GMPPCP or with fusidic acid and GDP, inhibits elongation factor Tu (EF Tu)-dependent binding of Phe-tRNA on the ribosome-poly(U) complex and binding of Ala-tRNA on the initiation complex formed with RNA from bacteriophage R17; GTP hydrolysis associated with Phe-tRNA binding is also inhibited. Moreover, nonenzymic binding of Phe-tRNA at ...
متن کاملInteraction of guanosine nucleotides with elongation factor 2. II. Effect of ribosomes and magnesium ions on guanosine diphosphate and guanosine triphosphate binding to the enzyme.
The effects of ribosomes and Mg-2plus on the binding of GDP and GTP to elongation factor 2 (EF-2) have been studied by an improved filter-binding assay. Both ribosomes and Mg-2plus strongly inhibit the binding of GDP but have apparently no effect on the GTP binding to the enzyme. An apparent stimulation by ribosomes of GTP binding to EF-2 is time-dependent and parallels a concomitant increase o...
متن کاملGlutamate-dependent phosphorylation of elongation factor-2 and inhibition of protein synthesis in neurons.
Postischemic delayed neuronal death is attributed to excitotoxic activation of glutamate receptors. It is preceded by a persistent inhibition of protein synthesis, the molecular basis of which is not known. Here we have examined in cortical neurons in culture the regulation by glutamate of phosphorylation of eukaryotic elongation factor-2 (eEF-2) by eEF-2 kinase, a Ca2+/calmodulin-dependent enz...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1975
ISSN: 0264-6021
DOI: 10.1042/bj1480447