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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.

Short Answer

Expert verified
There are 12 possible mRNA sequences coding for the tripeptide Leu-Met-Tyr.

Step by step solution

01

Understanding Genetic Code

Each amino acid is coded by a sequence of three nucleotides called a codon. Different codons can code for the same amino acid, a property known as 'degeneracy' of the genetic code.
02

Identifying Codons for Leucine (Leu)

Leucine is coded by six different codons: UUA, UUG, CUU, CUC, CUA, and CUG.
03

Identifying Codons for Methionine (Met)

Methionine is coded by a single codon: AUG. This simplifies our calculation for methionine in the sequence.
04

Identifying Codons for Tyrosine (Tyr)

Tyrosine is coded by two codons: UAC and UAU.
05

Calculating Total Possible Combinations

To find the number of different mRNA sequences that can code for the amino acid sequence Leu-Met-Tyr, multiply the number of codons for each amino acid: 6 (Leu) x 1 (Met) x 2 (Tyr). This yields 12 possible mRNA sequences.
06

Listing All Possible mRNA Sequences

- UUA-AUG-UAC - UUA-AUG-UAU - UUG-AUG-UAC - UUG-AUG-UAU - CUU-AUG-UAC - CUU-AUG-UAU - CUC-AUG-UAC - CUC-AUG-UAU - CUA-AUG-UAC - CUA-AUG-UAU - CUG-AUG-UAC - CUG-AUG-UAU

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Key Concepts

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

Amino Acids
Amino acids are the building blocks of proteins, which are essential molecules that perform a variety of functions in living organisms. There are 20 different standard amino acids used by cells to build proteins, each with unique properties. They encode specific functions due to their distinct side chains, which impact how they interact with each other and their environment.

In terms of the genetic code, amino acids are specified by sequences of three nucleotides in DNA or RNA, known as codons. For example, in the exercise provided, the amino acid sequence of Leucine (Leu), Methionine (Met), and Tyrosine (Tyr) is considered for its potential diversity of mRNA sequences.
  • Leucine is represented by six possible codons, showing it's highly flexible within the genetic code.
  • Methionine, meanwhile, has only one codon (AUG), which is unique because it's also the start codon in protein synthesis.
  • Tyrosine can be encoded by two different codons, providing some variation in the genetic code.
mRNA Sequences
Messenger RNA (mRNA) is a type of RNA that serves as a template for protein synthesis. It is synthesized based on the sequence of nucleotides in the DNA and is crucial for conveying the genetic information needed to form proteins.

Once DNA is transcribed into mRNA, this sequence reflects the future protein's blueprint. Each group of three nucleotide bases on mRNA corresponds to one amino acid in the chain. For instance, in our tripeptide of Leucine-Methionine-Tyrosine, the DNA is transcribed into various mRNA sequences. These mRNA sequences are read in sets of three bases called codons, which specify the realization of different amino acids, allowing for multiple mRNA versions that can produce the same protein sequence.
  • It is the mRNA that ultimately guides the synthesis of proteins during a process known as translation.
  • This demonstrates how genetic coding is translated into a physical amino acid sequence by reading the sequences of mRNA codons.
Codons
Codons are vital units of the genetic language composed of triplet nucleotide sequences found in mRNA. Each codon directs the incorporation of a specific amino acid into a growing polypeptide chain during protein synthesis. The genetic code is considered degenerate because several codons can encode the same amino acid.

In the exercise's example, codons for Leucine (Leu) exemplify this degeneracy, where six different codons (UUA, UUG, CUU, CUC, CUA, and CUG) can be used to code for Leucine. Methionine (Met), on the other hand, uses a single codon (AUG), while Tyrosine (Tyr) can be translated from two possible codons (UAC, UAU). This variability allows for robustness in genetic coding and potential error corrections in DNA.
  • Codons play a critical role in ensuring that proteins are synthesized accurately and efficiently.
  • This diversity ensures the protein synthesis machinery can tolerate some mutations without altering protein function.
  • Understanding how different codons translate into amino acids helps illustrate the genetic code's complexity and redundancy.
Polypeptide Synthesis
Polypeptide synthesis is the process by which cells construct proteins from amino acids, following the instructions encoded in the mRNA sequence. It is a central activity in biology that involves transcription and translation.

Transcription is the initial step where DNA's genetic code is copied into mRNA. Translation is where this mRNA is used as a guide to assemble amino acids into a polypeptide chain on ribosomes, the molecular machines responsible for protein assembly. Each codon on the mRNA correlates with specific transfer RNA (tRNA) molecules, which carry the corresponding amino acids and participate in forming the protein sequence.
  • During translation, the mRNA sequence is read step by step, codon by codon, ensuring each amino acid is added correctly to the growing chain.
  • Proteins begin to fold into their specific structures as they are synthesized, which determines their functionality in the organism.
  • Without the precise process of polypeptide synthesis, cells could not produce the proteins necessary for life and biological functions.

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Most popular questions from this chapter

Resistance of the Genetic Code to Mutation The RNA sequence shown represents the beginning of an open reading frame (ORF). What changes (if any) can occur at each position without generating a change in the encoded amino acid residue? (5')AUGAUAUUGCUAUCUUGGACU

Rate of Protein Synthesis A bacterial ribosome can synthesize about 20 peptide bonds per minute. If the average bacterial protein is approximately 260 amino acid residues long, how many proteins can the ribosomes in an \(E\). coli cell synthesize in 20 minutes if all ribosomes are functioning at maximum rates?

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?

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?

Bacterial Protein Export Bacteria mostly use the system shown in Eig \(27-44\) to export proteins out of the cell. SecB, one of the chaperone proteins found only in gram-negative bacteria, delivers a newly translated polypeptide to the SecA ATPase on the interior side of the membrane. SecA pushes the exported protein through a membrane pore formed by the SecYEG complex. The SecYEG complex is homologous to the Sec61 complex in eukaryotes. Which component of this bacterial protein export system would be the most attractive target for antibiotic development? Explain.

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