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Methionine Has Only One Codon Methionine is one of two amino acids with only one codon. How does the single codon for methionine specify both the initiating residue and the interior Met residues of polypeptides synthesized by \(E\). coli?

Short Answer

Expert verified
AUG codon serves both as an initiation signal with tRNA^fMet and as an interior Met residue marker with tRNA^Met.

Step by step solution

01

Understand Codons and Methionine

Methionine is an amino acid that is uniquely specified by only one codon, AUG, in the genetic code. This codon plays a crucial role in the initiation of protein synthesis.
02

Role of AUG Codon

The AUG codon serves a dual purpose: it codes for Methionine both as a starting signal for the ribosome to initiate protein synthesis, and as an indicator for the incorporation of Methionine into the interior of a protein chain. This versatility is integral to E. coli's polypeptide synthesis.
03

Mechanism of Initiation

In the initiation of protein synthesis in E. coli, the AUG codon is recognized by a special initiator tRNA called tRNA^fMet, which is modified to carry formyl-methionine (fMet). This distinct form allows the cell machinery to recognize the start of a protein.
04

Incorporation of Interior Methionine

When AUG codon appears in the middle of a mRNA sequence, it is recognized by a different tRNA, called tRNA^Met, that brings a regular Methionine to the growing peptide chain, differentiating it from the initiation role.

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Key Concepts

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

Methionine
Methionine is a special amino acid because it is one of the two amino acids that are specified by a single codon, which in this case is AUG. It holds an essential position in protein synthesis as it serves as the starting amino acid in nearly all newly synthesized polypeptide chains. Methionine is important not only because of its role as an initiator but also because it can be found within the interior of proteins.
  • Methionine's unique single-codon specification gives it a distinct function in biochemical processes.
  • It plays a vital role both at the initiation of protein synthesis and in various structural and functional parts of proteins once the initial synthesis is complete.
AUG Codon
The AUG codon is the genetic sequence that codes for methionine. Its significance extends beyond just coding for an amino acid. It serves a dual purpose in the genetic code.
  • Firstly, AUG acts as the start codon in mRNA, signaling the ribosome where to begin translating the genetic message into a protein.
  • Secondly, it is also used to code for methionine when it appears within a protein being synthesized.
This versatility ensures that proteins are synthesized correctly and that methionine is incorporated both as the initial segment and within the growing protein structure. The ability of the AUG codon to perform such distinct roles highlights the complexity and efficiency of genetic coding mechanisms.
Protein Synthesis
Protein synthesis is the process by which cells build proteins, and it begins with the role of methionine and the AUG codon. Upon encountering the AUG codon at the start of an mRNA strand, the ribosome initiates translation, commencing the assembly of a polypeptide chain.
  • This process begins with the recognition of the AUG codon as the start codon, marking the spot for the ribosomal machinery to assemble and start synthesizing the protein.
  • The initiation of protein synthesis is critically dependent on the presence of a specialized tRNA that aids in this process (tRNA^fMet in E. coli).
  • Methionine marks the beginning, but other amino acids soon follow, added by various tRNA molecules as the ribosome travels along the mRNA sequence.
Protein synthesis is fundamental for cell function and involves intricate processes that ensure proteins are built efficiently and accurately.
tRNA
Transfer RNA (tRNA) acts as an adapter molecule in protein synthesis, linking codons in the mRNA to the appropriate amino acids. It plays an essential role in ensuring proteins are built with the correct sequence of amino acids.
  • tRNA molecules have anticodons, which are complementary to codons in the mRNA. This allows them to bring the right amino acids to the ribosome for protein assembly.
  • In the case of methionine, two types of tRNA are involved: tRNA^fMet, which recognizes the start codon AUG and brings formyl-methionine to initiate protein synthesis, and tRNA^Met, which incorporates regular methionine into the peptide chain interior.
tRNA's ability to interpret the genetic code and deliver specific amino acids is crucial for the accuracy and effectiveness of protein synthesis. Each tRNA is specific to one amino acid, making it a vital player in translating genetic information into functional proteins.

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Most popular questions from this chapter

Predicting Anticodons from Codons Most amino acids have more than one codon and attach to more than one tRNA, each with a different anticodon. Write all possible anticodons for the four codons of glycine: \(\left(5^{\prime}\right) \mathrm{GGU}, \mathrm{GGC}\), GGA, and GGG. a. From your answer, which of the positions in the anticodons are primary determinants of their codon specificity in the case of glycine? b. Which of these anticodon-codon pairings has/have a wobbly base pair? c. In which of the anticodon-codon pairings do all three positions exhibit strong Watson-Crick hydrogen bonding?

Importance of the "Second Genetic Code" Some aminoacyl-tRNA synthetases do not recognize and bind the anticodon of their cognate tRNAs but instead use other structural features of the tRNAs to impart binding specificity. The tRNAs for alanine apparently fall into this category. a. What features of tRNA \(^{\text {Ala }}\) does Ala-tRNA synthetase recognize? b. Describe the consequences of a \(\mathrm{C} \rightarrow \mathrm{G}\) mutation in the third position of the anticodon of \(\mathrm{tRNA}^{\mathrm{Ala}}\). c. What other kinds of mutations might have similar effects? d. Mutations of these types are never found in natural populations of organisms. Why? (Hint: Consider what might happen both to individual proteins and to the organism as a whole.)

Synthetic mRNAs The genetic code was elucidated through the use of polyribonucleotides synthesized either enzymatically or chemically in the laboratory. Given what we now know about the genetic code, how would you make a polyribonucleotide that could serve as an mRNA coding predominantly for many Phe residues and for a small number of Leu and Ser residues? What other amino acid(s) would be encoded by this polyribonucleotide, but in smaller amounts?

The Direction of Protein Synthesis In 1961, Howard Dintzis established that protein synthesis on ribosomes begins at the amino terminus and proceeds toward the carboxyl terminus. He used immature red blood cells that were still synthesizing hemoglobin. He added radioactively labeled leucine (chosen because it occurs frequently in both the \(a\) and \(\beta\) subunits) for various lengths of time, rapidly isolated only the full-length (completed) \(a\) subunits, and then determined where in the peptide the labeled amino acids were located. After the labeled leucine and extract had been incubated together for one hour, the protein was labeled uniformly along its length. However, after much shorter incubation times, the labeled amino acids were clustered at one end. At which end, amino or carboxyl terminus, did Dintzis find the labeled residues after the short exposure to labeled leucine?

How Many Different mRNA Sequences Can Specify One Amino Acid Sequence? Write all the possible mRNA sequences that can code for the simple tripeptide segment Leu-Met-Tyr. Your answer will give you some idea of the number of possible mRNAs that can code for one polypeptide.

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