In e. coli, the elongation factor EF-Tu forms part of a Eu-Tu-GTP--tRNA complex
ID: 59862 • Letter: I
Question
In e. coli, the elongation factor EF-Tu forms part of a Eu-Tu-GTP--tRNA complex and increases the rate of tRNA-mRNA binding. GTP hydrolysis to GDP and Pi also enables a type of kinetic proofreading, which prevents the addition of an incorrect amino acid to the growing peptide chain.
Determine which of the following statements are true. Check all the true statements.
In E. coli, the elongation factor EF-Tu forms part of an EF-Tu-GTP-tRNA complex and increases the rate of tRNA-mRNA binding. GTP hydrolysis to GDP and Pi also enables a type of kinetic proofreading, which prevents the addition of an incorrect amino acid to the growing peptide chain. Determine which of the following statements are true. Check all the true statements. A mismatch between the codon and anticodon creates a distortion in the mRNA-tRNA complex. pcorrect match between the codon and anticodon causes a conformational change in the small sonal sa hitanee ads todo and an sido causes a conformational change in the small in riposomal subunit and leads to GTP hydrolysis. Hydrolysis of GTP associated with EF-Tu frees the peptidyl-tRNA for peptide bond formation. Hydrolysis of GTP associated with EF-Tu brings about a conformational change in the amino acid. A mismatch between the codon and anticodon does not cause conformational changes, and the Ef-Tu-GTP-aminoacyl-tRNA complex leaves the ribosome before a peptide bond can form If the mRNA codon and tRNA anticodon match, EF-Tu-GDP leaves the ribosome.Explanation / Answer
The correct answers are :
Reason: EF-TU-GTP attaches to aminocyl tRNA complex and matches it with mRNA codon.This brings a conformational change in ribosome and GTP hydrolysis occurs and a peptide bond is formed between the aminoacids.EF-TU-GDP now leaves the ribosome.EF-TU-GDP is exchanged with GTP in cytoplasm to carry another aminocyl t-RNA complex to ribosome.
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