Ef-Tu

Definition

ef-Tu is a bacterial elongation factor that plays a critical role in the process of translation, specifically in the delivery of aminoacyl-tRNA to the ribosome during protein synthesis. This factor is essential for ensuring that the correct amino acid is added to the growing polypeptide chain, thereby maintaining the fidelity of translation. The interaction of ef-Tu with GTP also highlights its role in regulating the overall efficiency and accuracy of protein synthesis.

5 Must Know Facts For Your Next Test

1. ef-Tu binds to GTP when it is inactive and to aminoacyl-tRNA, facilitating its delivery to the ribosome during translation.
2. Once the correct codon-anticodon pairing occurs at the ribosomal A site, ef-Tu hydrolyzes GTP to GDP, leading to a conformational change that releases the aminoacyl-tRNA for peptide bond formation.
3. The activity of ef-Tu is critical for maintaining translational accuracy, as incorrect aminoacyl-tRNA binding can lead to misincorporation of amino acids into proteins.
4. In bacteria, ef-Tu operates in conjunction with another elongation factor called ef-G, which assists in translocating the ribosome along the mRNA after peptide bond formation.
5. The presence of antibiotics can target ef-Tu or disrupt its function, highlighting its importance in bacterial translation and making it a potential target for antibiotic therapy.

Review Questions

• How does ef-Tu contribute to the accuracy of protein synthesis during translation?
  • ef-Tu contributes to the accuracy of protein synthesis by binding to aminoacyl-tRNA and delivering it to the ribosome, ensuring that the correct amino acid is incorporated based on codon-anticodon pairing. This process reduces errors during translation as only those tRNAs with complementary sequences can successfully bind. The hydrolysis of GTP upon correct pairing further ensures that only accurate tRNAs are used, making ef-Tu a crucial player in maintaining fidelity.
• Discuss how the interaction between ef-Tu and GTP influences its role in protein synthesis.
  • The interaction between ef-Tu and GTP is vital for its function in protein synthesis. When ef-Tu binds GTP, it forms a complex with aminoacyl-tRNA, enabling efficient delivery to the ribosome. Upon successful codon-anticodon matching at the ribosome's A site, ef-Tu hydrolyzes GTP to GDP, which causes a conformational change that releases the tRNA for incorporation into the growing polypeptide chain. This mechanism not only regulates translation but also enhances its speed and accuracy.
• Evaluate the potential implications of targeting ef-Tu with antibiotics on bacterial translation and overall cell function.
  • Targeting ef-Tu with antibiotics could significantly disrupt bacterial translation by interfering with aminoacyl-tRNA delivery and leading to an increase in translational errors. Such disruption would impair protein synthesis essential for bacterial growth and survival. Additionally, since ef-Tu plays a regulatory role in translation efficiency, antibiotics that inhibit its function may slow down overall bacterial metabolism and increase susceptibility to other stressors. This approach could be beneficial in developing new antibiotics that specifically target bacterial systems without affecting eukaryotic cells.

Related terms

Aminoacyl-tRNA: Aminoacyl-tRNA is a molecule that consists of a specific amino acid attached to its corresponding transfer RNA (tRNA), which is responsible for delivering the amino acid to the ribosome during translation.

Ribosome: The ribosome is a complex molecular machine found within all living cells that facilitates the translation of messenger RNA (mRNA) into polypeptides by orchestrating the assembly of amino acids.

GTPase: GTPases are enzymes that hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP), playing key roles in cellular signaling and protein synthesis, including the function of elongation factors like ef-Tu.