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What does EF-Tu and EF-G do?
An excellent example is the mechanism of the elongation cycle in protein synthesis, that uses the elongation factor Tu (EF-Tu) to deliver aminoacyl-tRNA (aa-tRNA) to the mRNA-programmed ribosome, and the elongation factor G (EF-G) to help the translocation of the tRNA–mRNA complex on the ribosome.
What is the function of EF-G in protein translation?
EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in protein translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
What does EF-G bind to?
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.
What does EF-Tu Do?
Elongation factor thermal unstable Tu (EF-Tu) is a G protein that catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome inside living cells. Structural and biochemical studies have described the complex interactions needed to effect canonical function.
Why is EF-Tu so important in E coli?
EF-Tu recognizes common features of tRNAs and also that the tRNA is aminoacylated. EF-Tu is one of the most abundant proteins in bacteria, often present as 5% of the total cell protein. In Escherichia coli, there are more than five molecules of EF-Tu per ribosome, and most of the aa-tRNA in the cell is bound to EF-Tu.
Why does EF-Tu hydrolyze GTP?
In each round of ribosomal translation, the translational GTPase elongation factor Tu (EF-Tu) delivers a transfer RNA (tRNA) to the ribosome. After successful decoding, EF-Tu hydrolyzes GTP, which triggers a conformational change that ultimately results in the release of the tRNA from EF-Tu.
Where is EF-G located?
The 30S subunit is on the left and 50S subunit is on the right. EF-G is directly visible and seen to interact with both 30S and 50S subunits (6, 7). The tip of the elongated portion of EF-G is situated in the neck region of 30S subunit, where the anticodon loop region of A site tRNA binds (11, 12).
Does translation start at the 5 end?
Translation does not simply begin at the 5´ end of the mRNA; it starts at specific initiation sites. The 5´ terminal portions of both prokaryotic and eukaryotic mRNAs are therefore noncoding sequences, referred to as 5´ untranslated regions.
What is EF-Tu made of?
EF-Tu is suggested to consist of three domains: 1 (amino acids 1–200), 2 (amino acids 208–295), and 3 (amino acids 298–394) (36), all of them participating in ternary complex formation. The 3′-CCA-Phe, the 5′ end, and the T-stem of tRNA are shown to be involved in the interaction with EF-Tu in the complex (34).
What is the function of EF-G in protein elongation?
Function in protein elongation EF-G catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation. In this process, the peptidyl transferase center (PTC) has catalyzed the formation of a peptide bond between amino acids, moving the polypeptide chain from the P site tRNA to the A site tRNA.
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Are there any paralogous versions of the EF-G factor?
EF-G has a complex evolutionary history, with numerous paralogous versions of the factor present in bacteria, suggesting subfunctionalization of different EF-G variants. Elongation factors exist in all three domains of life with similar function on the ribosome. The eukaryotic and archeal homologs of EF-G are eEF2 and aEF2, respectively.
What does EF stand for in a dictionary?
EF – What does EF stand for? The Free Dictionary Also found in: Dictionary, Thesaurus, Medical, Encyclopedia, Wikipedia . Copyright 1988-2018 AcronymFinder.com, All rights reserved. Want to thank TFD for its existence? Tell a friend about us, add a link to this page, or visit the webmaster’s page for free fun content .