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Chapter 30: Problem 16

How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?

Short Answer

Expert verified
Four ATP equivalents are consumed for each amino acid added to the elongating polypeptide chain during protein synthesis.

Step by step solution

01

tRNA charging

tRNA charging (aminoacylation) is the first step where an amino acid is linked to its corresponding tRNA. ATP is used in this critical step to provide the energy required for the formation of the aminoacyl-tRNA complex. Two ATP molecules are consumed for each amino acid being attached to a tRNA molecule.
02

Elongation phase of protein synthesis

After the formation of the aminoacyl-tRNA complex, the elongation phase of protein synthesis begins. Here, each aminoacyl-tRNA (except for the initiator) binds to an A site. The peptide chain then increases by one amino acid unit. To power this process, the power from one GTP molecule (which is equivalent to ATP in energy) is used.
03

Translocation

Once a new peptide bond is formed, the ribosome moves, or 'translocates,' to read the next codon of mRNA. This requires another GTP. Hence, each cycle of elongation consumes an equivalent of two ATPs during tRNA charging and two more equivalents (from GTPs) during elongation and translocation. So for each amino acid added, we consume a total of four ATP equivalents.

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Most popular questions from this chapter

In the protein synthesis elongation events described under the section on translocation, which of the following seems the most apt account of the peptidyl transfer reaction: (a) The peptidyl-tRNA delivers its peptide chain to the newly arrived aminoacyl-tRNA situated in the A site, or (b) the aminoacyl end of the aminoacyl-tRNA moves toward the \(P\) site to accept the peptidyl chain? Which of these two scenarios makes more sense to you? Why?

Eukaryotic ribosomes are larger and more complex than prokaryotic ribosomes. What advantages and disadvantages might this greater ribosomal complexity bring to a eukaryotic cell?

Review the evidence establishing that aminoacyl-tRNA synthetases bridge the information gap between amino acids and codons. Indicate the various levels of specificity possessed by aminoacyl-tRNA synthetases that are essential for high-fidelity translation of messenger RNA molecules.

What ideas can you suggest to explain why ribosomes invariably exist as two- subunit structures, instead of a larger, single-subunit entity?

Point out why Crick's wobble hypothesis would allow fewer than 61 anticodons to be used to translate the 61 sense codons. How might "wobble" tend to accelerate the rate of translation?
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