Elongation factor G (EF-G) (EF-G)

Elongation factor G (EF-G), encoded by the fusA gene, is a vital GTPase that facilitates the translocation of mRNA and tRNAs within the bacterial ribosome during the elongation phase of protein synthesis [1, 8]. By hydrolyzing GTP, EF-G provides the energy necessary to move the ribosome one codon forward, ensuring the accurate and rapid assembly of polypeptides [1, 6]. Beyond elongation, EF-G is also essential for ribosome recycling, collaborating with the ribosome recycling factor (RRF) to dissociate the ribosomal subunits after protein release [17, 19]. Due to its indispensable role in bacterial growth, EF-G is a major target for antibiotics, most notably fusidic acid, which traps the factor on the ribosome in a GDP-bound state [4, 7]. This immobilization halts protein production, leading to bacteriostatic or bactericidal effects [4, 11]. Resistance to EF-G inhibitors typically involves mutations in the fusA gene, which can alter drug binding or factor kinetics, presenting a challenge in treating infections like those caused by Staphylococcus aureus [4, 7].

Other names

TranslocasefusA gene productPeptide elongation factor GEF-G1EF-G2

Inhibition of protein synthesis by stabilizing the EF-G-GDP-ribosome complex, preventing translocation and factor dissociation (e.g., fusidic acid), or by interfering with EF-G binding to the GTPase-associated center (e.g., thiopeptides).