fusA Antibody

1. Kinetics of spontaneous and EF-G-accelerated rotation of ribosomal subunits has been presented. PMID: 27524615
2. These results show that EF-G bound to GTP (EF-G-GTP) continuously samples both rotational states of the ribosome, binding with higher affinity to the rotated state. PMID: 23624862
3. These structures suggest that EF-G controls the translocation reaction by cycles of conformational rigidity and relaxation before and after GTP hydrolysis. PMID: 23812721
4. A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation PMID: 21531717
5. the structure of the rRNA stabilized by the C-terminal domain of L11 is necessary to stabilize EF-G binding in the post-translocation state, and thiostrepton may modulate this structure in a manner that interferes with the ribosome-EF-G interaction PMID: 15492007
6. control of Pi release by interactions between EF-G and L7/12 appears to be important for maintaining the conformational coupling between EF-G and the ribosome for translocation and for timing the dissociation of the factor from the ribosome PMID: 16292341
7. These results imply that during the GTP hydrolytic cycle EF-G must detach from S12 within the central cavity of the ribosome, while EF-G can remain associated with L7/L12 located on one of the peripheral stalks of the ribosome. PMID: 17395204
8. Binding of elongation factor EF-G in the presence of nonhydrolyzable GTP analog GDPNP stabilizes the 70S ribosome intermediate hybrid state; complete translocation is supported only by EF-G.GTP or EF-G.GDPNP. PMID: 17630323
9. Single-molecule studies for ribosomes engaged in poly(Phe) synthesis, fluor. res. energy transfer (FRET) between the G' domain of EF-G and the N-terminal domain of protein L11 occurs within two rapidly interconverting states. PMID: 17727272
10. Collectively, the results support a central role of sw1 in driving the EF-G cycle during protein synthesis. PMID: 19536129

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KEGG: ecj:JW3302

STRING: 316385.ECDH10B_3515