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One remarkable feature of the genetic code is that amino acids with similar chemical properties often have similar codons. Thus codons with U or \(C\) as the second nucleotide tend to specify hydrophobic amino acids. Can you suggest a possible explanation for this phenomenon in terms of the early evolution of the protein-synthesis machinery?

Short Answer

Expert verified
Early protein synthesis may have been error-prone, so similar codons for similar amino acids minimized harmful effects of mistranslation.

Step by step solution

01

Identify Key Concept

Recognize that the codon arrangement tends to place similar amino acids near each other, which may be useful for early evolution in minimizing errors during protein synthesis.
02

Consider Chemical Properties

Note that U or C as the second nucleotide often corresponds to codons for hydrophobic amino acids. These similar chemical properties might help stabilize protein structures.
03

Evolutionary Advantage

Consider how having similar codons for similar amino acids could decrease the impact of translation errors, as a single point mutation might still produce an amino acid with similar properties.
04

Molecular Explanation

Contemplate that early protein-synthesis machinery might have been less accurate, so having similar codons for similar amino acids could offset potential errors and result in functional proteins despite translation mistakes.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Codon Arrangement
The genetic code is a system in which genetic information is translated into proteins. One intriguing aspect of this code is the systematic arrangement of codons, the sequences of three nucleotides that correspond to specific amino acids. In the genetic code, amino acids with similar properties often have similar codons. This systematic arrangement can be beneficial in reducing errors during protein synthesis.
This concept of codon arrangement is thought to play a key role in the early evolution of life. If a single point mutation occurs in the DNA, changing one base pair, it's likely that it might still result in a similar amino acid. Thus, this arrangement minimizes the effect of translation errors on protein synthesis.
  • A mutation in the third position of the codon (known as "wobble position") often results in no change in the amino acid.
  • Mutations in other positions might lead to amino acids with similar chemical properties.
This strategic arrangement would have provided an evolutionary advantage, ensuring functional proteins despite errors that were more common in early, less accurate molecular machinery.
Hydrophobic Amino Acids
Amino acids are the building blocks of proteins, and they can be categorized based on their chemical properties. Some amino acids are hydrophobic, meaning they do not interact well with water. Hydrophobic amino acids play a vital role in maintaining the structure and function of proteins.
In the genetic code, codons with U or C as the second nucleotide frequently code for hydrophobic amino acids. This is significant because:
  • Hydrophobic amino acids often participate in creating the protein's core, away from the aqueous environment.
  • They contribute to the stability and folding of proteins, ensuring that they maintain the correct shape required for their function.
The tendency for certain codons to specify hydrophobic amino acids reflects an evolutionary optimization. By grouping these codons, the genetic code reduces the likelihood of errors impacting the protein's hydrophobic center, which is crucial for maintaining its integrity and functionality.
Protein Synthesis Accuracy
The accuracy of protein synthesis is crucial for producing functional proteins. The genetic code has evolved features that enhance the fidelity of protein synthesis, especially in the early stages of evolution when molecular machinery was less accurate.
During protein synthesis, ribosomes translate the mRNA codons into a sequence of amino acids. The reliability of this process is supported by several mechanisms:
  • Redundancy in the genetic code (multiple codons for a single amino acid) helps mitigate translation errors.
  • Similar codons for similar amino acids ensure that point mutations are less likely to result in detrimental effects on protein function.
The ability of early organisms to produce proteins accurately despite a higher propensity for errors was likely a significant evolutionary advantage. This ensured that even when mistakes occurred, the resulting proteins could still retain their functional properties, thereby aiding the survival and reproduction of the organism.

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Most popular questions from this chapter

Which of the following types of mutations would be predicted to harm an organism? Explain your answers. A. Insertion of a single nucleotide near the end of the coding sequence. B. Removal of a single nucleotide near the beginning of the coding sequence. C. Deletion of three consecutive nucleotides in the middle of the coding sequence. D. Deletion of four consecutive nucleotides in the middle of the coding sequence. E. Substitution of one nucleotide for another in the middle of the coding sequence.

The Lacheinmal protein is a hypothetical protein that causes people to smile more often. It is inactive in many chronically unhappy people. The mRNA isolated from a number of different unhappy individuals in the same family was found to lack an internal stretch of 173 nucleotides that is present in the Lacheinmal mRNA isolated from happy members of the same family. The DNA sequences of the Lacheinmal genes from the happy and unhappy family members were determined and compared. They differed by a single nucleotide substitution, which lay in an intron. What can you say about the molecular basis of unhappiness in this family? (Hints: [1] Can you hypothesize a molecular mechanism by which a single nucleotide substitution in a gene could cause the observed deletion in the mRNA? Note that the deletion is internal to the mRNA. [2] Assuming the 173 -base-pair deletion removes coding sequences from the Lacheinmal mRNA, how would the Lacheinmal protein differ between the happy and unhappy people?)

Could the RNA polymerase used for transcription also be used to make the RNA primers required for DNA replication (discussed in Chapter 6 )?

Discuss the following: "During the evolution of life on Earth, RNA lost its glorious position as the first selfreplicating catalyst. Its role now is as a mere messenger in the information flow from DNA to protein."

A. The average molecular weight of a protein in the cell is about 30,000 daltons. A few proteins, however, are much larger. The largest known polypeptide chain made by any cell is a protein called titin (made by mammalian muscle cells), and it has a molecular weight of 3,000,000 daltons. Estimate how long it will take a muscle cell to translate an mRNA coding for titin (assume the average molecular weight of an amino acid to be \(120,\) and a translation rate of two amino acids per second for eukaryotic cells). B. Protein synthesis is very accurate: for every 10,000 amino acids joined together, only one mistake is made. What is the fraction of average-sized protein molecules and of titin molecules that are synthesized without any errors? [Hint: the probability \(P\) of obtaining an error-free protein is given by \(P=(1-E)^{n},\) where \(E\) is the error frequency and \(n\) the number of amino acids.] C. The combined molecular weight of the eukaryotic ribosomal proteins is about \(2.5 \times 10^{6}\) daltons. Would it be advantageous to synthesize them as a single protein? D. Transcription occurs at a rate of about 30 nucleotides per second. Is it possible to calculate the time required to synthesize a titin mRNA from the information given here?

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