Gene Expression 2: RNA Translation Overview
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Questions and Answers

What is translation in the context of gene expression?

Translation is the process of converting the nucleotide sequence of mRNA into an amino acid sequence, resulting in the synthesis of proteins.

How does tRNA facilitate translation?

tRNA serves as an adapter molecule that recognizes specific amino acids on one end and their corresponding codons on the other end, ensuring accurate translation.

What roles do ribosomes play during translation?

Ribosomes coordinate the interaction between mRNA, tRNA, enzymes, and protein factors required for protein synthesis.

Explain the concept of degeneration in the genetic code.

<p>The genetic code is degenerate because multiple codons can specify the same amino acid, except for tryptophan and methionine, which have unique codons.</p> Signup and view all the answers

What is the significance of the start codon AUG in translation?

<p>AUG serves as the start codon that initiates the translation process, coding for the amino acid methionine.</p> Signup and view all the answers

Define the 'wobble theory' in relation to genetic code.

<p>The wobble theory suggests that the third nucleotide in a codon is less crucial than the first two in determining the specific amino acid.</p> Signup and view all the answers

Identify the three stop codons in the genetic code.

<p>The three stop codons are UAA, UAG, and UGA, which signal the termination of translation.</p> Signup and view all the answers

Describe the direction in which the genetic information in mRNA is read.

<p>The genetic information along mRNA is read in the 5’ to 3’ direction during translation.</p> Signup and view all the answers

What role does the anticodon play in protein biosynthesis?

<p>The anticodon pairs with a specific codon on the mRNA within the ribosome to ensure the correct amino acid is added during translation.</p> Signup and view all the answers

What is the significance of the initiation complex in protein biosynthesis?

<p>The initiation complex is formed by the association of the ribosomal subunits with mRNA and initiation factors, marking the beginning of translation.</p> Signup and view all the answers

How does gTP hydrolysis contribute to the binding of aminoacyl-tRNA to the A site?

<p>GTP hydrolysis provides the energy required for the binding of the activated aminoacyl-tRNA to the A site of the ribosome.</p> Signup and view all the answers

What distinguishes the genetic code as non-overlapping and commaless?

<p>The genetic code is read continuously in groups of three bases (codons) without any punctuation or overlap between them.</p> Signup and view all the answers

List the components required for initiation of protein biosynthesis.

<p>The components required include mRNA, tRNA, rRNA, eukaryotic initiation factors (eIFs), GTP, ATP, and various amino acids.</p> Signup and view all the answers

Explain the concept of tRNA charging.

<p>tRNA charging is the process of attaching a specific amino acid to the 3' hydroxyl end of a tRNA molecule through an ester linkage.</p> Signup and view all the answers

Describe the significance of the universal nature of the genetic code.

<p>The universal nature of the genetic code indicates that the same code words are used to specify amino acids across all organisms, promoting conservation in biological processes.</p> Signup and view all the answers

What are the three binding sites for tRNA on the ribosome, and what does each site do?

<p>The three binding sites are the A site (aminoacyl), P site (peptidyl), and E site (exit). The A site binds incoming aminoacyl-tRNA, the P site holds the growing peptide chain, and the E site releases empty tRNA.</p> Signup and view all the answers

What is the role of the first codon on mRNA during translation?

<p>The first codon on mRNA codes for methionine, which initiates the peptide sequence.</p> Signup and view all the answers

Describe the function of the peptidyl transferase enzyme during peptide bond formation.

<p>Peptidyl transferase catalyzes the formation of a peptide bond by facilitating the transfer of the alpha amino group from an amino acid in the A site to the carboxylic group of the tRNA in the P site.</p> Signup and view all the answers

What is the significance of the GTP and eEF-2 in the translocation process?

<p>GTP and eEF-2 are responsible for the translocation of the newly formed peptidyl-tRNA from the A site to the P site after peptide bond formation.</p> Signup and view all the answers

What occurs when a stop codon appears in the A site during translation termination?

<p>The stop codon prompts releasing factors (eRFs) to recognize the termination signal, leading to the hydrolysis of the bond between the peptide chain and tRNA in the P site.</p> Signup and view all the answers

How many high-energy phosphate bonds are utilized in the formation of one peptide bond?

<p>The formation of one peptide bond requires the hydrolysis of 4 high-energy phosphate bonds.</p> Signup and view all the answers

Explain the role of molecular chaperones in protein maturation.

<p>Molecular chaperones assist in the proper folding of proteins into their three-dimensional structures.</p> Signup and view all the answers

What are the potential outcomes of errors in translation?

<p>Errors in translation can result in faulty proteins, which may be targeted for degradation or could function abnormally.</p> Signup and view all the answers

What are the three components involved in releasing the peptide chain from the tRNA during termination?

<p>The releasing factors (eRFs), GTP, and peptidyl transferase facilitate the release of the peptide chain from the tRNA.</p> Signup and view all the answers

What is the significance of proteolysis in post-translational processing of proteins?

<p>Proteolysis is crucial as it removes specific amino acid sequences, including signal peptides, which facilitates the correct localization and function of proteins.</p> Signup and view all the answers

How does hydroxylation of proline and lysine contribute to collagen synthesis?

<p>Hydroxylation of proline and lysine is essential for collagen stability as it allows for the formation of cross-links within collagen fibers.</p> Signup and view all the answers

Explain the role of glycosylation in the stability of glycoproteins.

<p>Glycosylation stabilizes glycoproteins by attaching carbohydrate side chains that protect them from degradation and assist in proper folding.</p> Signup and view all the answers

What are the potential clinical implications of protein synthesis inhibitors like tetracyclines?

<p>Protein synthesis inhibitors, such as tetracyclines, can effectively combat bacterial infections by disrupting bacterial protein translation.</p> Signup and view all the answers

How does phosphorylation affect cell signaling processes?

<p>Phosphorylation of amino acids like serine, threonine, or tyrosine modulates protein activity, influencing various signaling pathways.</p> Signup and view all the answers

What effect does acylation have on protein function?

<p>Acylation alters protein function by adding fatty acids, aiding in membrane anchoring and influencing cellular localization.</p> Signup and view all the answers

Describe the mechanism by which diphtheria toxin inhibits protein synthesis.

<p>Diphtheria toxin inhibits eukaryotic translation by binding to eukaryotic elongation factor 2 (EF-2), preventing translocation during protein synthesis.</p> Signup and view all the answers

What role does γ-carboxylation of glutamic acid play in prothrombin and osteocalcin?

<p>γ-Carboxylation of glutamic acid is essential for calcium binding, which is critical for the blood clotting process in prothrombin and bone ossification in osteocalcin.</p> Signup and view all the answers

What specific amino acid is associated with the initiation codon AUG during protein biosynthesis?

<p>Methionine</p> Signup and view all the answers

In the elongation stage, what happens to GTP when aminoacyl-tRNA binds to the A site?

<p>GTP is hydrolyzed.</p> Signup and view all the answers

What are the two eukaryotic initiation factors that bind to the 40S subunit during the initiation of translation?

<p>eIF-1 and eIF-3</p> Signup and view all the answers

During the initiation of protein biosynthesis, how is the tRNA charged?

<p>By attaching a specific amino acid to the 3' hydroxyl adenosine terminus of tRNA in an ester linkage.</p> Signup and view all the answers

What role does the ribosomal P site play during peptide bond formation?

<p>It holds the tRNA carrying the growing polypeptide chain.</p> Signup and view all the answers

What is meant by the term 'degeneracy' in the context of the genetic code?

<p>Degeneracy refers to the feature where multiple codons can specify the same amino acid, except for tryptophan and methionine, which are each coded by only one codon.</p> Signup and view all the answers

How does the 'wobble theory' explain the specificity of codons in amino acid incorporation?

<p>The wobble theory suggests that the third nucleotide in a codon is less critical for specifying an amino acid, allowing for redundancy in codon usage while maintaining the integrity of protein synthesis.</p> Signup and view all the answers

Describe the difference between start and stop codons in the context of translation.

<p>Start codons, like AUG, initiate translation, signaling the beginning of protein synthesis, while stop codons (UAA, UAG, UGA) signal the termination of the process.</p> Signup and view all the answers

What is the significance of reading the genetic information in mRNA from 5' to 3'?

<p>Reading from 5' to 3' ensures proper translation of codons into amino acids and maintains the correct polarity of the newly synthesized protein.</p> Signup and view all the answers

What role does the specificity of tRNA play in the accuracy of translation?

<p>tRNA's specificity ensures that each amino acid is matched correctly to its corresponding codon on the mRNA, minimizing errors during protein synthesis.</p> Signup and view all the answers

Flashcards

Translation

The process of converting the nucleotide sequence of mRNA, into an amino acid sequence of a protein to create proteins.

Genetic Code

The set of rules by which information encoded in genetic material (DNA or mRNA sequences) is translated into proteins (amino acid sequences).

Codon

A sequence of three nucleotides that specifies a particular amino acid or stop signal during protein synthesis.

Start Codon

The codon (AUG) that signals the beginning of protein synthesis, specifying the amino acid methionine.

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Stop Codons

Codons (UAA, UAG, UGA) that signal the end of protein synthesis.

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mRNA

Messenger RNA; carries the genetic information from DNA to the ribosome for protein synthesis.

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tRNA

Transfer RNA; an adapter molecule that carries amino acids to the ribosome during protein synthesis, matching codons to the correct amino acid.

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Ribosomes

Cellular organelles that coordinate the interaction between mRNA, tRNA, enzymes and protein factors during protein synthesis.

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Degenerate Genetic Code

Multiple codons can code for the same amino acid.

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Wobble Hypothesis

The third nucleotide in a codon is less important in determining the amino acid than the first two.

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Unambiguous Genetic Code

Each codon specifies only one particular amino acid.

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Codon

A three-nucleotide sequence on mRNA that specifies a particular amino acid.

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Start Codon

The first codon on mRNA, always coding for methionine.

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Peptide Bond Formation

The linking of two amino acids, forming a peptide chain, catalyzed by peptidyl transferase.

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Peptidyl Transferase

The enzyme (ribozyme) that catalyzes peptide bond formation.

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Translocation

The movement of the tRNA with the growing peptide chain from the A site to the P site.

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Stop Codon

A codon (UAA, UAG, or UGA) that signals the end of protein synthesis.

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Release Factors

Proteins that recognize stop codons and terminate translation.

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Protein Maturation

The processes that transform a newly synthesized polypeptide chain into a functional protein.

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Protein Folding

The process by which a polypeptide chain assumes its 3D structure, aided by chaperones.

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tRNA

Transfer RNA, carries amino acids to the ribosome during protein synthesis.

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Proteolysis

Removal of amino-terminal, carboxy-terminal, or internal sequences from proteins.

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Signal Peptides

Sequences that guide proteins to their final destinations and are then removed.

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Hydroxylation

Adding a hydroxyl group to proline and lysine; important for collagen.

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Phosphorylation

Adding a phosphate group to serine, threonine, or tyrosine - crucial in cell signaling.

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γ-carboxylation

Adding a γ-carboxyl group to glutamic acid; important for calcium binding for clotting and bone formation.

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Glycosylation

Adding carbohydrate chains (CHO) to proteins creating glycoproteins. Improves stability and proper conformation.

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N-linked glycosylation

Attachment of carbohydrate chains to asparagine.

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O-linked glycosylation

Attachment of carbohydrate chains to serine and threonine.

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Acylation

Adding fatty acids to various amino acids, creating membrane anchors.

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Genetic Code

A set of rules specifying how a sequence of nucleotide triplets (codons) in a nucleic acid sequence (e.g., DNA or RNA) is translated into a sequence of amino acids in a polypeptide (protein).

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Codon

A sequence of three nucleotides that codes for a specific amino acid or stop signal during protein synthesis.

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Non-overlapping code

Codons are read independently and sequentially without any overlap between them.

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Commaless code

The genetic code is read continuously without any punctuation or spaces between codons.

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Universal genetic code

The same codons specify the same amino acids in all organisms.

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Protein Biosynthesis

The process of creating proteins from amino acid building blocks based on the genetic code.

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Initiation (protein synthesis)

The first stage of protein synthesis, involving the assembly of ribosomes and other factors required for polypeptide chain initiation.

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Elongation (protein synthesis)

The process of sequentially adding amino acids to the growing polypeptide chain.

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Termination (protein synthesis)

The final stage of protein synthesis, where the polypeptide chain synthesis is stopped.

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tRNA

Transfer RNA; a type of RNA molecule that carries amino acids to the ribosome during protein synthesis.

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rRNA

Ribosomal RNA; a type of RNA that, together with proteins, makes up ribosomes.

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mRNA

Messenger RNA; a type of RNA that carries the genetic code from DNA to the ribosome.

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eukaryotic initiation factors (eIFs)

Proteins that help initiate translation in eukaryotic cells.

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tRNA charging

The process of attaching a specific amino acid to a tRNA molecule.

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Anticodon

A three-nucleotide sequence on a tRNA molecule that is complementary to a codon on mRNA.

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Ribosome

Complex molecular machine that carries out protein synthesis in all living cells.

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A site

One of the three binding sites on a ribosome for tRNA.

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P site

One of the three binding sites on a ribosome for tRNA.

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E site

One of the three binding sites on a ribosome for tRNA.

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Genetic Code

Relationship of mRNA codons (3 nucleotides) to amino acids in protein synthesis.

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Translation

Converting mRNA's nucleotide sequence to an amino acid sequence (protein).

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Codon

Three-nucleotide sequence on mRNA that specifies an amino acid.

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Start Codon

AUG codon, specifies methionine and protein synthesis start.

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Stop Codons

UAA, UAG, UGA codons; signal the end of protein synthesis.

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Degenerate Genetic Code

Multiple codons can code for the same amino acid (except Trp & Met).

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Wobble Hypothesis

Third mRNA base is less critical in specifying amino acids.

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mRNA

Carries genetic information from DNA to ribosomes for protein creation.

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tRNA

Transfer RNA; carries amino acids to ribosomes, matching codons.

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Ribosomes

Cellular structures that coordinate mRNA, tRNA, and protein factors in translation.

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Genetic Code Non-overlapping

Codons are read individually and sequentially without overlap.

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Genetic Code Commaless

Codons are read continuously without any punctuation.

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Genetic Code Universal

The same codons specify the same amino acids in all organisms.

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Protein Biosynthesis Initiation

The start of protein production, assembling ribosome, and mRNA.

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Protein Biosynthesis Elongation

The process of extending the polypeptide chain.

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Protein Biosynthesis Termination

The final step, stopping protein building.

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tRNA Charging

Attaching an amino acid to a tRNA molecule.

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Anticodon

The three-base sequence on tRNA matching a codon.

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eukaryotic initiation factor (eIF)

Protein helpers in eukaryotic translation initiation.

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eukaryotic ribosome 80S

The ribosome in eukaryotic cells, made of 40S and 60S subunits

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A, P, and E sites

Binding locations for tRNA in the ribosome during translation.

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Study Notes

Gene Expression 2: RNA Translation and Genetic Code

  • Learning Objectives (ILOs):
    • Discuss the rules of the genetic code.
    • Correlate the function of different RNAs in the translation process.
    • Describe the process of translation.
    • Interpret the role of translation and post-translational modification in health and disease.

What is Translation?

  • Translation is the process of converting the nucleotide sequence of mRNA (codons) into an amino acid sequence of a protein for protein synthesis.
  • Codons are sequences of three nucleotides.
  • The genetic code is the collection of codons that correspond to specific amino acids.
  • Proteins are made from a 20-letter amino acid language translated from the 4-letter nucleic acid language.

Requirements of Translation

  • mRNA: Carries the genetic information.
  • tRNA: An adapter molecule that recognizes amino acids and their corresponding codons. Each amino acid has at least one specific type of tRNA.
  • Ribosomes: Molecular machines that coordinate the interaction between mRNA, tRNA, enzymes, and protein factors for protein synthesis.

Genetic Code (Figure 1)

  • The genetic code is the relationship between the nucleotide sequence of DNA or mRNA, and the amino acids in a polypeptide chain.
  • Each amino acid can be specified by more than one codon.
  • There is one start codon (AUG-Methionine).
  • There are three stop codons (UAA, UAG, UGA).
  • The genetic information on mRNA is read from the 5' to 3' direction.

Characteristics of the Genetic Code

  • Degenerate: Multiple codons can code for the same amino acid (except tryptophan and methionine).
  • Unambiguous: Each codon specifies only one amino acid.
  • Non-overlapping and Commaless: The code is read from a fixed starting point as a continuous sequence of codons, taken three at a time.
  • Universal: The same code words are used in all organisms (prokaryotes and eukaryotes).

Protein Biosynthesis Stages

  • Initiation: The process of ribosome assembly. Initiation involves ribosomes, mRNA, tRNA, GTP, ATP, and various initiation factors.
  • Elongation: The process of adding amino acids to the growing polypeptide chain. Elongation involves tRNA binding, peptide bond formation, and translocation.
  • Termination: The process of stopping polypeptide synthesis. The stop codon is recognized by release factors, and the polypeptide chain is released.

N.B: tRNA Charging (Figure 3)

  • tRNA charging is how specific amino acids are attached to tRNA, forming aminoacyl-tRNA. This involves enzymes and ATP.

Stage 2: Elongation

  • Binding of aminoacyl-tRNA to the A site. The ribosome has three sites (A, P, and E) for tRNA molecules. An aminoacyl-tRNA binds to the A site.
  • Peptide bond formation. The alpha amino group of the incoming amino acid attacks the carboxylic group of the peptidyl-tRNA in the P site, forming a new peptide bond. This reaction is catalyzed by peptidyl transferase.
  • Translocation. The ribosome moves along the mRNA, shifting the peptidyl-tRNA from the A site to the P site, and the discharged tRNA to the E site.

Stage 3: Termination

  • The appearance of a stop codon on the mRNA in the A site initiates the termination of translation.
  • Release factors recognize the stop codons in the A site, triggering the hydrolysis of the bond between the polypeptide chain and the tRNA in the P site.
  • The ribosome subunits dissociate, releasing all components of the complex.

N.B: The formation of one peptide bond requires hydrolysis of 4 high-energy phosphate bonds (in various steps).

Protein Maturation

  • Proteins are modified post-translationally (after they are synthesized) to achieve their final functional form. Modifications can include folding, localization in the cell, modifications of individual amino acids (e.g., glycosylation, hydroxylation, phosphorylation).

Proteins and Clinical Implications

  • Many antibiotics target bacterial protein synthesis.
  • Some toxins inhibit eukaryotic translation, leading to serious diseases or death.

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Explore the intricacies of RNA translation and the genetic code in this quiz. Understand the roles of mRNA and tRNA in protein synthesis, and learn about translation and post-translational modifications. Dive into how these processes impact health and disease.

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