Conformational Control of the Interaction of Eukaryotic Elongation Factors EF-1 and EF-2 with Ribosomes
نویسندگان
چکیده
منابع مشابه
Conformational control in EF-hand proteins
The ability to manipulate ligand-induced conformational change, although representing a major challenge to the protein engineer, is an essential end point in efforts to produce novel functional proteins for biotechnology and therapeutic applications. Progress towards this goal requires determining not only what factors control the fold and stability of a protein, but also how ligand binding alt...
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Evidence for two species of elongation factor 1 (EF 1(A) and EF 1(B)) from calf brain has been obtained by molecular sieve chromatography on Sephadex G-150. A high molecular weight form, EF 1(A), interacts with GTP to form an EF 1(A)-GTP complex. GDP also reacts with EF 1, but unlike the reaction with GTP, an EF 1(B)-GDP complex is formed that contains a lower molecular weight and labile specie...
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Protein elongation factors, EF-Tu and EF-1a, have been implicated in cell response to heat stress. We investigated the expression (accumulation) of EF-Tu and EF-1a in mature plants of spring wheat cultivars Kukri and Excalibur, and tested the hypothesis that cultivars with contrasting tolerance to heat stress differ in the accumulation of these elongation factors under prolonged exposure to hig...
متن کاملInteraction of animal mitochondrial EF-Tu.EF-Ts with aminoacyl-tRNA, guanine nucleotides, and ribosomes.
The mammalian mitochondrial complex consisting of elongation factors EF-Tu and EF-Ts (EF-Tu.Tsmt) is capable of efficiently binding aminoacyl-tRNA to the ribosome in the presence and absence of guanine nucleotides. In the presence of GTP the binding reaction is catalytic. In the absence of guanine nucleotides, or in the presence of a non-hydrolyzable GTP analog, only one round of ribosome bindi...
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 ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1973
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.70.12.3556