Review Translational dynamics

Nygård, Odd; Nilsson, Lars

doi:10.1007/978-3-642-76168-3_9

Cited by 6 publications

(7 citation statements)

References 266 publications

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“…ADP-R-F2 GTPase r was competitively inhibited by GDP, and the value of KЈ i was identical to that determined with not ADP-ribosylated SsEF-2. Therefore, the ADP-ribosylation of SsEF-2 does not affect the binding of GDP and GTP to SsEF-2; a similar finding has been reported for rat liver EF-2 (22).…”

Section: Affinity Of Ssef-2 For Guanosine Nucleotides In the Presencesupporting

confidence: 84%

Studies on the Polypeptide Elongation Factor 2 from Sulfolobus solfataricus

Raimo

Bocchini

1995

Journal of Biological Chemistry

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The elongation factor 2 from the thermoacidophilic archaeon Sulfolobus solfataricus (SsEF-2) binds [ In the course of the protein synthesis the translocation of the peptidyl-tRNA from the A-site to the P-site of the ribosome is catalyzed in eubacteria by the elongation factor G and in eukarya and archaea by the elongation factor 2, both in the GTP-bound form. Following the interaction of the elongation factor-GTP complex with the ribosome, the GTP is hydrolyzed to GDP and P i , and the inactive GDP bound form of EF-2/EF-G

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Section: Affinity Of Ssef-2 For Guanosine Nucleotides In the Presencesupporting

confidence: 84%

Studies on the Polypeptide Elongation Factor 2 from Sulfolobus solfataricus

Raimo

Bocchini

1995

Journal of Biological Chemistry

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“…This could allow initial binding and GTP hydrolysis, which has been shown for EF-G to be a very early event in translocation (5). Other reports have indicated a marked decrease in the ability of ADPR-eEF2 to associate with the 80 S ribosome (32)(33)(34)(35) as well as a significant reduction in binding and hydrolysis of GTP upon ADP-ribosylation (32,35). Furthermore, ADPR-eEF2 binds weaker than eEF2 to a synthetic oligonucleotide (SRD RNA) mimicking the sarcin/ricin loop of 28 S ribosomal RNA (51).…”

Section: Discussionmentioning

confidence: 89%

Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae

Jørgensen

Yates

Teal

et al. 2004

Journal of Biological Chemistry

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The crystal structure of ADP-ribosylated yeast elongation factor 2 in the presence of sordarin and GDP has been determined at 2.6 Å resolution. The diphthamide at the tip of domain IV, which is the target for diphtheria toxin and Pseudomonas aeruginosa exotoxin A, contains a covalently attached ADP-ribose that functions as a very potent inhibitor of the factor. We have obtained an electron density map of ADP-ribosylated translation factor 2 revealing both the ADP-ribosylation and the diphthamide. This is the first structure showing the conformation of an ADP-ribosylated residue and confirms the inversion of configuration at the glycosidic linkage. Binding experiments show that the ADP-ribosylation has limited effect on nucleotide binding affinity, on ribosome binding, and on association with exotoxin A. These results provide insight to the inhibitory mechanism and suggest that inhibition may be caused by erroneous interaction of the translation factor with the codon-anticodon area in the P-site of the ribosome.

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“…However, the results presented here and the established role of EF-la as a major act&binding protein [2,10] strongly suggest a possible regulatory link between the protein synthesizing machinery and cytoskeleton. The much higher cellular content of actin [23] is possibly balanced by the higher affinity of EF-2 in its ribosomal interactions [24,25]. In this context, an about twofold excess of EF-2 over ribosomes in the cell deserves special consideration [26-281, and our own unpublished results).…”

Section: Discussionmentioning

confidence: 98%

Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton

Bektaş¹,

Nurten²,

Gurel³

et al. 1994

FEBS Letters

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Eukaryotic elongation factor 2 (EF-2) was shown to bind to F-a&n as assayed by co-sedimentation. In the presence of guanosine-5'-O-(3-thiotriphosphate) (GTPyS) binding was increased fourfold. At saturation level a molar ratio of about 0.12 EF-2 per F-a&n (subunit) was observed. Our results suggest a single type of binding site with an apparent dissociation constant of 0.85 PM. The stoichiometry was independent of the filament length, and ADP-ribosylation had no effect on the binding. Experimental data indicated the involvement of SH-groups of both EF-2 and actin in the binding. The interaction EF-2 with F-a&in appeared to be inhibited competitively by EF-la and non-competitively by G-actin.

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Review Translational dynamics

Cited by 6 publications

References 266 publications

Studies on the Polypeptide Elongation Factor 2 from Sulfolobus solfataricus

Studies on the Polypeptide Elongation Factor 2 from Sulfolobus solfataricus

Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae

Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton

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