The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G

2019 ◽  
Vol 87 (8) ◽  
pp. 699-705
Author(s):  
Biswaranjan Mohanty ◽  
Paulina Hanson‐Manful ◽  
Thomas J. Finn ◽  
Cecilia R. Chambers ◽  
James L. O. McKellar ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Bacterial Protein ◽  
Elongation Factor G ◽  
Domain Iii ◽  
Factor G

scholarly journals Elongation factor G initiates translocation through a power stroke

2016 ◽  
Vol 113 (27) ◽  
pp. 7515-7520 ◽  
Author(s):  
Chunlai Chen ◽  
Xiaonan Cui ◽  
John F. Beausang ◽  
Haibo Zhang ◽  
Ian Farrell ◽  
...  
Keyword(s):  
Single Molecule ◽  
Messenger Rna ◽  
Elongation Factor ◽  
Power Stroke ◽  
Elongation Factor G ◽  
Gtp Hydrolysis ◽  
Guanosine Triphosphatase ◽  
Prokaryotic Protein ◽  
Domain Iii ◽  
Factor G

During the translocation step of prokaryotic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (GTPase), binds to the ribosomal PRE-translocation (PRE) complex and facilitates movement of transfer RNAs (tRNAs) and messenger RNA (mRNA) by one codon. Energy liberated by EF-G’s GTPase activity is necessary for EF-G to catalyze rapid and precise translocation. Whether this energy is used mainly to drive movements of the tRNAs and mRNA or to foster EF-G dissociation from the ribosome after translocation has been a long-lasting debate. Free EF-G, not bound to the ribosome, adopts quite different structures in its GTP and GDP forms. Structures of EF-G on the ribosome have been visualized at various intermediate steps along the translocation pathway, using antibiotics and nonhydolyzable GTP analogs to block translocation and to prolong the dwell time of EF-G on the ribosome. However, the structural dynamics of EF-G bound to the ribosome have not yet been described during normal, uninhibited translocation. Here, we report the rotational motions of EF-G domains during normal translocation detected by single-molecule polarized total internal reflection fluorescence (polTIRF) microscopy. Our study shows that EF-G has a small (∼10°) global rotational motion relative to the ribosome after GTP hydrolysis that exerts a force to unlock the ribosome. This is followed by a larger rotation within domain III of EF-G before its dissociation from the ribosome.

Crystallographic study of the large tryptic fragments of elongation factor G from Escherichia coli

1982 ◽  
Vol 160 (1) ◽  
pp. 127-132 ◽  
Author(s):  
Ludmila S. Reshetnikova ◽  
Marina B. Garber ◽  
Natalia P. Fomenkova ◽  
Stanislav V. Nikonov ◽  
Yuri N. Chirgadze
Keyword(s):  
Escherichia Coli ◽  
Elongation Factor ◽  
Elongation Factor G ◽  
Crystallographic Study ◽  
Factor G

scholarly journals The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State

Science ◽  
2009 ◽  
Vol 326 (5953) ◽  
pp. 694-699 ◽  
Author(s):  
Y.-G. Gao ◽  
M. Selmer ◽  
C. M. Dunham ◽  
A. Weixlbaumer ◽  
A. C. Kelley ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Elongation Factor G ◽  
Factor G

A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaeteBorrelia burgdorferi

2010 ◽  
Vol 75 (6) ◽  
pp. 1445-1454 ◽  
Author(s):  
Takuma Suematsu ◽  
Shin-ichi Yokobori ◽  
Hiroyuki Morita ◽  
Shigeo Yoshinari ◽  
Takuya Ueda ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Elongation Factor G ◽  
Factor G
Sign in / Sign up

Export Citation Format

Share Document