Differential Modulation of the Elongation-Factor-G GTPase Activity by tRNA Bound to the Ribosomal A-Site or P-Site

1982 ◽  
Vol 125 (2) ◽  
pp. 415-421 ◽  
Author(s):  
Gianni CHINALI ◽  
Andrea PARMEGGIANI
Keyword(s):  
Elongation Factor ◽  
Gtpase Activity ◽  
Differential Modulation ◽  
Elongation Factor G ◽  
A Site ◽  
Factor G

scholarly journals Active role of elongation factor G in maintaining the mRNA reading frame during translation

2019 ◽  
Vol 5 (12) ◽  
pp. eaax8030 ◽  
Author(s):  
Bee-Zen Peng ◽  
Lars V. Bock ◽  
Riccardo Belardinelli ◽  
Frank Peske ◽  
Helmut Grubmüller ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Active Role ◽  
Transfer Rna ◽  
Specific Interactions ◽  
Elongation Factor G ◽  
Reading Frame ◽  
A Site ◽  
Factor G ◽  
Domain 4

During translation, the ribosome moves along the mRNA one codon at a time with the help of elongation factor G (EF-G). Spontaneous changes in the translational reading frame are extremely rare, yet how the precise triplet-wise step is maintained is not clear. Here, we show that the ribosome is prone to spontaneous frameshifting on mRNA slippery sequences, whereas EF-G restricts frameshifting. EF-G helps to maintain the mRNA reading frame by guiding the A-site transfer RNA during translocation due to specific interactions with the tip of EF-G domain 4. Furthermore, EF-G accelerates ribosome rearrangements that restore the ribosome’s control over the codon-anticodon interaction at the end of the movement. Our data explain how the mRNA reading frame is maintained during translation.

scholarly journals Conformationally Restricted Elongation Factor G Retains GTPase Activity but Is Inactive in Translocation on the Ribosome

2000 ◽  
Vol 6 (2) ◽  
pp. 501-505 ◽  
Author(s):  
Frank Peske ◽  
Natalia B. Matassova ◽  
Andreas Savelsbergh ◽  
Marina V. Rodnina ◽  
Wolfgang Wintermeyer
Keyword(s):  
Elongation Factor ◽  
Gtpase Activity ◽  
Elongation Factor G ◽  
Conformationally Restricted ◽  
Factor G

scholarly journals Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Gabriel Demo ◽  
Howard B. Gamper ◽  
Anna B. Loveland ◽  
Isao Masuda ◽  
Christine E. Carbone ◽  
...  
Keyword(s):  
16S Rrna ◽  
Elongation Factor ◽  
Structural Basis ◽  
Elongation Factor G ◽  
Ribosomal Frameshifting ◽  
Elongation Cycle ◽  
70S Ribosome ◽  
Complex Features ◽  
A Site ◽  
Factor G

AbstractFrameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven ~3.5-Å-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G•GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.

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