scholarly journals The role of GTP in transient splitting of 70S ribosomes by RRF (ribosome recycling factor) and EF-G (elongation factor G)

2008 ◽  
Vol 36 (21) ◽  
pp. 6676-6687 ◽  
Author(s):  
G. Hirokawa ◽  
N. Iwakura ◽  
A. Kaji ◽  
H. Kaji
Keyword(s):  
Elongation Factor ◽  
Ribosome Recycling Factor ◽  
Elongation Factor G ◽  
Factor G

scholarly journals The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G in Staphylococcus aureus

2020 ◽  
Vol 295 (18) ◽  
pp. 6053-6063 ◽  
Author(s):  
Arnab Basu ◽  
Kathryn E. Shields ◽  
Mee-Ngan F. Yap
Keyword(s):  
Staphylococcus Aureus ◽  
Stress Responses ◽  
Alternative Pathway ◽  
Heat Exposure ◽  
Elongation Factor ◽  
Normal Growth ◽  
Ribosome Recycling Factor ◽  
Elongation Factor G ◽  
Independent Manner ◽  
Factor G

The formation of translationally inactive 70S dimers (called 100S ribosomes) by hibernation-promoting factor is a widespread survival strategy among bacteria. Ribosome dimerization is thought to be reversible, with the dissociation of the 100S complexes enabling ribosome recycling for participation in new rounds of translation. The precise pathway of 100S ribosome recycling has been unclear. We previously found that the heat-shock GTPase HflX in the human pathogen Staphylococcus aureus is a minor disassembly factor. Cells lacking hflX do not accumulate 100S ribosomes unless they are subjected to heat exposure, suggesting the existence of an alternative pathway during nonstressed conditions. Here, we provide biochemical and genetic evidence that two essential translation factors, ribosome-recycling factor (RRF) and GTPase elongation factor G (EF-G), synergistically split 100S ribosomes in a GTP-dependent but tRNA translocation-independent manner. We found that although HflX and the RRF/EF-G pair are functionally interchangeable, HflX is expressed at low levels and is dispensable under normal growth conditions. The bacterial RRF/EF-G pair was previously known to target only the post-termination 70S complexes; our results reveal a new role in the reversal of ribosome hibernation that is intimately linked to bacterial pathogenesis, persister formation, stress responses, and ribosome integrity.

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 Activation of GTP hydrolysis in mRNA-tRNA translocation by elongation factor G

2015 ◽  
Vol 1 (4) ◽  
pp. e1500169 ◽  
Author(s):  
Wen Li ◽  
Zheng Liu ◽  
Ravi Kiran Koripella ◽  
Robert Langlois ◽  
Suparna Sanyal ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Elongation Factor G ◽  
Direct Role ◽  
Gtp Hydrolysis ◽  
Ribosomal Subunits ◽  
Trna Translocation ◽  
Gtpase Activation ◽  
Guanosine Triphosphatase ◽  
Factor G

During protein synthesis, elongation of the polypeptide chain by each amino acid is followed by a translocation step in which mRNA and transfer RNA (tRNA) are advanced by one codon. This crucial step is catalyzed by elongation factor G (EF-G), a guanosine triphosphatase (GTPase), and accompanied by a rotation between the two ribosomal subunits. A mutant of EF-G, H91A, renders the factor impaired in guanosine triphosphate (GTP) hydrolysis and thereby stabilizes it on the ribosome. We use cryogenic electron microscopy (cryo-EM) at near-atomic resolution to investigate two complexes formed by EF-G H91A in its GTP state with the ribosome, distinguished by the presence or absence of the intersubunit rotation. Comparison of these two structures argues in favor of a direct role of the conserved histidine in the switch II loop of EF-G in GTPase activation, and explains why GTP hydrolysis cannot proceed with EF-G bound to the unrotated form of the ribosome.

scholarly journals Release of Ribosome-bound Ribosome Recycling Factor by Elongation Factor G

2003 ◽  
Vol 278 (48) ◽  
pp. 48041-48050 ◽  
Author(s):  
Michael C. Kiel ◽  
V. Samuel Raj ◽  
Hideko Kaji ◽  
Akira Kaji
Keyword(s):  
Elongation Factor ◽  
Ribosome Recycling Factor ◽  
Elongation Factor G ◽  
Factor G

scholarly journals The Role of Guanosine Triphosphate in Translocation Reaction Catalyzed by Elongation Factor G

1974 ◽  
Vol 249 (13) ◽  
pp. 4321-4323
Author(s):  
Noriko Inoue-Yokosawa ◽  
Chikako Ishikawa ◽  
Yoshito Kaziro
Keyword(s):  
Elongation Factor ◽  
Guanosine Triphosphate ◽  
Elongation Factor G ◽  
Factor G
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