EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in mRNA translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome. [1]

2010年2月7日 · EF-G is generally viewed as the factor required for the translocation step of protein biosynthesis. Two forms of EF-Gmt are observed in mitochondrial systems [114,115]. EF-G1 mt is involved in translocation while EF-G2 mt appears to be used primarily during termination (see Section 4.3).

2013年12月23日 · Ribosomal translocation and back-translocation refer to the forward and backward movements of the tRNA 2 –mRNA complex on the ribosome during elongation. Elongation factor G (EF-G) catalyses...

2016年6月16日 · 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 …

EF-G, EF4, and BipA are members of the translation factor family of GTPases with a common ribosome binding mode and GTPase activation mechanism. However, topological variations of shared as well as unique domains ensure different roles …

2015年12月2日 · During translation, elongation factor G (EF-G) plays a catalytic role in tRNA translocation and a facilitative role in ribosome recycling.

2009年10月10日 · Elongation factor G (EF-G) is a GTPase that plays a crucial role in the translocation of tRNAs and mRNA during translation by the ribosome. We report a crystal structure refined to 3.6 Å resolution of the ribosome trapped with EF-G in the post-translocational state using the antibiotic fusidic acid.

2022年11月11日 · Surprisingly, we find that blockage of GTP hydrolysis by the elongation factor G (EF-G) specifically abolishes reverse rotation of the head domain of the small ribosomal subunit, an event that occurs after translocation of the transfer RNA and messenger RNA is essentially complete.

1994年9月1日 · Two recent reports [1], [2] of the structure of the elongation factor-G (EF-G) bring us one step closer to understanding the ribosomal machinery at the atomic level. EF-G is a cytoplasmic factor which catalyzes the translocation step, …

Fusidic acid (FA), an antibiotic used against pathogenic bacteria Staphylococcus aureus, locks elongation factor-G (EF-G) to the ribosome after GTP hydrolysis. To clarify the mechanism of fitness loss and compensation in relation to FA resistance, we have characterized three S. aureus EF-G mutants with fast kinetics and crystal structures.