A researcher analyzes a collection of translation mutants for defects in GTP hydrolysis. She finds three bacterial mutants with this defect due to mutations in translation factors IF2, EF‑Tu, and EF‑G. In each case, the mutation allows for proper protein folding and the binding of GTP, but GTP hydrolysis is blocked.

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Danielle

Biology

7 November, 19:17

A researcher analyzes a collection of translation mutants for defects in GTP hydrolysis. She finds three bacterial mutants with this defect due to mutations in translation factors IF2, EF‑Tu, and EF‑G. In each case, the mutation allows for proper protein folding and the binding of GTP, but GTP hydrolysis is blocked.

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Giovanny Blankenship · Answer 1

IF-2: The 70S ribosome would form, but initiation factors would not be released and elongation could not start. EF-Tu: The second aminoacyl-tRNA would bind to the ribosomal A site, but no peptide bond would form. EF-G: The first peptide bond would form, but the ribosome would not not move along the mRNA to vacate the A site for binding of a new EF-TU-tRNA.