EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes.[2][3][4] It is found in eukaryotic mitochondria as TUFM.[5]
As a family of elongation factors, EF-Tu also includes its eukaryotic and archaeal homolog, the alpha subunit of eEF-1 (EF-1A).
^"TIGR00485: EF-Tu". National Center for Biotechnology Information. March 3, 2017.
^Yamamoto H, Qin Y, Achenbach J, Li C, Kijek J, Spahn CM, Nierhaus KH (February 2014). "EF-G and EF4: translocation and back-translocation on the bacterial ribosome". Nature Reviews. Microbiology. 12 (2): 89–100. doi:10.1038/nrmicro3176. PMID24362468. S2CID27196901.
^Ling M, Merante F, Chen HS, Duff C, Duncan AM, Robinson BH (Nov 1997). "The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene". Gene. 197 (1–2): 325–36. doi:10.1016/S0378-1119(97)00279-5. PMID9332382.