Protein Synthesis Quiz - Biology 101

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Questions and Answers

Which of the following is NOT a component required for protein synthesis?

  • Amino acids
  • Ribosomes
  • tRNA
  • DNA (correct)

What is the function of aminoacyl-tRNA synthetase?

  • It helps to elongate the polypeptide chain.
  • It catalyzes the attachment of an amino acid to its corresponding tRNA. (correct)
  • It helps to terminate the translation process.
  • It helps to initiate the translation process.

Which type of ribosome synthesizes proteins that are destined for secretion?

  • Free ribosomes
  • Membrane-bound ribosomes (correct)
  • Polysomes
  • All of the above

What is the role of tRNA in translation?

<p>It carries amino acids to the ribosome. (D)</p> Signup and view all the answers

What is a polysome?

<p>A group of ribosomes translating a single mRNA molecule. (B)</p> Signup and view all the answers

Which of the following is a characteristic of free ribosomes?

<p>They synthesize proteins that remain in the cytosol. (C)</p> Signup and view all the answers

Which of the following is NOT a post-translational modification of polypeptide chains?

<p>Transcription (C)</p> Signup and view all the answers

What is the role of ribosomes in translation?

<p>They catalyze the formation of peptide bonds between amino acids. (D)</p> Signup and view all the answers

In eukaryotes, what is the specific function of the 5' cap on mRNA during initiation?

<p>The 5' cap interacts with initiation factors and assists in the binding of the 40S ribosomal subunit to the mRNA. (C)</p> Signup and view all the answers

What is the difference in the initiation complex between prokaryotes and eukaryotes?

<p>All of the above (D)</p> Signup and view all the answers

What is the role of the Shine-Dalgarno sequence in prokaryotic translation initiation?

<p>It serves as a recognition site for the 30S ribosomal subunit, aligning the ribosome with the start codon. (C)</p> Signup and view all the answers

Which of the following statements accurately describes the relationship between transcription and translation in prokaryotes?

<p>Translation can start before transcription is completed. (C)</p> Signup and view all the answers

Which molecule is directly responsible for carrying the first amino acid to the ribosome in the initiation complex?

<p>tRNA (C)</p> Signup and view all the answers

What is the role of GTP in the initiation process of translation?

<p>Providing energy for the assembly of the initiation complex. (D)</p> Signup and view all the answers

What is the function of initiation factors in translation?

<p>They help assemble the initiation complex and promote the recruitment of the initiator tRNA. (D)</p> Signup and view all the answers

What is the difference between the initiator tRNA in bacteria and in mitochondria?

<p>Bacteria use a formylated methionine, while mitochondria use a regular methionine. (D)</p> Signup and view all the answers

What role do aminoacyl-tRNA synthetases play in protein synthesis?

<p>They covalently attach amino acids to specific tRNA molecules. (A)</p> Signup and view all the answers

What is the function of the proofreading activity of aminoacyl-tRNA synthetases?

<p>To remove incorrectly charged amino acids. (D)</p> Signup and view all the answers

Which of the following components are essential for peptide synthesis?

<p>Peptide elongation factors and energy sources like ATP and GTP. (B)</p> Signup and view all the answers

What is released when ATP is cleaved during the aminoacylation process?

<p>AMP and inorganic pyrophosphate. (C)</p> Signup and view all the answers

Which molecule is recognized by aminoacyl-tRNA synthetases for the attachment of amino acids?

<p>Uncharged tRNA. (B)</p> Signup and view all the answers

How many amino acids require specific enzymes for attachment to tRNA?

<ol start="20"> <li>(C)</li> </ol> Signup and view all the answers

Which of the following correctly identifies the carrier of amino acids in protein synthesis?

<p>tRNA. (C)</p> Signup and view all the answers

What is released during the formation of aminoacyl-tRNA from the adenylated amino acid?

<p>PPi and AMP. (B)</p> Signup and view all the answers

What initiates the translocation process during protein synthesis?

<p>GTP hydrolysis (A)</p> Signup and view all the answers

Which site does the uncharged tRNA move to during translocation?

<p>E site (D)</p> Signup and view all the answers

What is the result of hydrolysis of the bond linking the peptide to tRNA during termination?

<p>The nascent protein is released (C)</p> Signup and view all the answers

When does protein synthesis terminate?

<p>Upon reaching a stop codon (A)</p> Signup and view all the answers

Which codons are recognized by release factors to induce termination?

<p>Termination codons (A)</p> Signup and view all the answers

What is the role of eIF-2 in the regulation of translation in eukaryotes?

<p>Its phosphorylation leads to inactivation (A)</p> Signup and view all the answers

Which site on the ribosome is exposed for the next amino acyl tRNA after translocation?

<p>A site (B)</p> Signup and view all the answers

What happens to mRNA and ribosomal subunits during the termination step?

<p>They are released from the ribosome (B)</p> Signup and view all the answers

What is the role of the initiator tRNA during the initiation of protein synthesis?

<p>It carries a non-formylated methionine. (A)</p> Signup and view all the answers

During elongation, what is the main role of elongation factors?

<p>To assist in the binding of the correct aminoacyl-tRNA. (A)</p> Signup and view all the answers

Which of the following statements accurately describes the three steps of elongation?

<p>Translocation involves moving the ribosome from the 5′-end to the 3′-end. (D)</p> Signup and view all the answers

How does the ribosome ensure that the correct amino acid is added during protein synthesis?

<p>Using codon recognition by aminoacyl-tRNA. (A)</p> Signup and view all the answers

Which component of the ribosome transfers the amino acid from the P site to the A site?

<p>Peptidyl transferase. (A)</p> Signup and view all the answers

What is the purpose of GTP hydrolysis during the elongation phase?

<p>To facilitate the translocation of the ribosome. (A)</p> Signup and view all the answers

What does each amino acid in a protein correspond to?

<p>A codon. (B)</p> Signup and view all the answers

Which of the following processes is NOT involved in the initiation of protein synthesis?

<p>Elongation of the peptide chain. (C)</p> Signup and view all the answers

Which of the following is an example of a protein modification that involves the addition of a carbohydrate chain?

<p>Glycosylation (A)</p> Signup and view all the answers

What is the primary function of a signal sequence in a newly synthesized polypeptide?

<p>To direct the protein to its final destination within the cell (C)</p> Signup and view all the answers

Which of the following is a key enzyme involved in the removal of signal sequences from proteins?

<p>Peptidase (B)</p> Signup and view all the answers

Which type of post-translational modification is often used to target proteins to lysosomes?

<p>Glycosylation (A)</p> Signup and view all the answers

What is the role of ubiquitin in protein degradation?

<p>Ubiquitin attaches to proteins that are destined for rapid turnover, marking them for destruction by the proteasome. (D)</p> Signup and view all the answers

Which of the following post-translational modifications primarily affects the activity of enzymes?

<p>Phosphorylation (D)</p> Signup and view all the answers

Which of the following post-translational modifications is most likely to occur in the endoplasmic reticulum?

<p>Glycosylation (C), Hydroxylation (D)</p> Signup and view all the answers

Which of the following is NOT involved in protein degradation?

<p>Ribosome (B)</p> Signup and view all the answers

Flashcards

Amino Acids

The building blocks of proteins. All 20 amino acids must be present for protein synthesis to occur.

Ribosomes

Cellular structures responsible for protein synthesis. Composed of proteins and ribosomal RNA (rRNA).

tRNA (Transfer RNA)

Special delivery trucks that carry specific amino acids to the ribosomes. There are at least 31 tRNAs in humans, each carrying a specific amino acid.

Aminoacyl-tRNA Synthetase

Enzymes that attach the correct amino acid to its corresponding tRNA. This process creates the aminoacyl tRNA complex, which is ready to be used in protein synthesis.

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Free Ribosomes

Ribosomes that float freely in the cytoplasm. They synthesize proteins that stay within the cell or travel to specific locations like the nucleus.

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Membrane-Bound Ribosomes

Ribosomes attached to the endoplasmic reticulum (ER). They produce proteins that will be secreted from the cell or integrated into cellular membranes.

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Polysomes

Multiple ribosomes translating a single mRNA molecule simultaneously. This speeds up protein synthesis in cells with high demand.

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Translation

The process of converting the genetic code in mRNA into a protein. It involves three main steps: initiation, elongation, and termination.

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Aminoacylation

The process where an aminoacyl-tRNA synthetase attaches an amino acid to its corresponding tRNA molecule, creating a 'charged' tRNA ready for translation. This process requires energy from ATP.

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Fidelity of Synthetase Enzyme

The ability of aminoacyl-tRNA synthetases to recognize both the amino acid and its specific tRNA, ensuring accuracy in protein synthesis. This includes proofreading mechanisms to correct errors if the wrong amino acid is attached.

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rRNA (Ribosomal RNA)

RNA molecules that form the structural core of ribosomes. They are essential for the catalytic activity of the ribosome.

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mRNA (Messenger RNA)

Messenger RNA, which carries the genetic code from the DNA in the nucleus to the ribosomes in the cytoplasm, providing the instructions for protein synthesis.

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Translation Initiation

The process of initiating protein synthesis where the ribosome binds to mRNA and the first tRNA carrying methionine joins the complex.

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Shine-Dalgarno Sequence

A purine-rich sequence located 6-10 bases upstream of the AUG start codon in mRNA. It acts as a binding site for the ribosome in prokaryotes.

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Initiation Codon

The first codon in a messenger RNA (mRNA) sequence that specifies the start of protein synthesis, typically AUG.

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Initiator tRNA

A special tRNA that carries the first amino acid, methionine, to the ribosome during translation initiation.

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Initiation Factor

A specialized protein that helps initiate protein synthesis by bringing together the ribosome, mRNA, and the first tRNA.

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Translation Elongation

The process in which the ribosome moves along the mRNA strand, reading codons and adding corresponding amino acids to the growing polypeptide chain.

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Translation Termination

The process that signals the end of translation, where the ribosome reaches a stop codon on the mRNA, releasing the newly synthesized polypeptide chain.

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Transcription

The process by which genetic information encoded in DNA is transcribed into messenger RNA (mRNA), which then serves as a template for protein synthesis.

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Codon

A set of three nucleotides on mRNA that specifies a particular amino acid.

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Transfer RNA (tRNA)

A special molecule that delivers the correct amino acid to the ribosome during translation.

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A site

The specific site on a ribosome where the incoming aminoacyl-tRNA binds during translation.

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P site

The site on a ribosome where the growing polypeptide chain is held during translation.

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Peptide Bond Formation

The process of adding an amino acid to the growing polypeptide chain during translation.

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Signal Sequence

A short sequence of amino acids that directs a newly synthesized protein to its correct location within the cell, like a postal code.

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Post-translational Modification

The process of modifying a protein after its synthesis is complete, often to activate it or target it to a specific location.

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Trimming or Proteolytic Cleavage

The removal of a portion of a protein, usually a signal sequence, to activate it or make it functional.

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Phosphorylation

The attachment of phosphate groups to a protein, often affecting its activity or function.

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Glycosylation

The attachment of sugar molecules to a protein, affecting its stability, location, or function.

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Hydroxylation

The addition of a hydroxyl group to amino acids like proline and lysine, often important for collagen structure.

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Ubiquitination

The process of tagging a protein with ubiquitin, marking it for degradation by the proteasome.

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Proteasome

A cellular 'recycling center' that breaks down proteins tagged with ubiquitin.

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Where does tRNA get the energy for charging?

The energy required for attaching an amino acid to a tRNA molecule comes from ATP.

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What is translocation in translation?

The movement of the ribosome along the mRNA molecule by three nucleotides in the 3' direction, following peptide bond formation.

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What is a stop codon in translation?

A sequence of three nucleotides on mRNA that signals the end of protein synthesis, causing the ribosome to detach from the mRNA and release the newly formed polypeptide chain.

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What are release factors in translation?

Proteins that bind to stop codons and cause the release of the polypeptide chain from the ribosome, ending translation.

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What is post-translational modification of proteins?

The process of modifying a protein after its synthesis, often involving chemical modifications like phosphorylation or glycosylation.

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What is translation regulation?

The control of protein synthesis by regulating the initiation and elongation of translation. It is a crucial step in the precise control of cellular functions.

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How is translation regulated in eukaryotes?

In eukaryotes, translation is regulated by covalent modification of eukaryotic initiation factor 2 (eIF-2), which can become inactive when phosphorylated. In addition, certain proteins can bind to mRNA and either inhibit its use by blocking translation or extend its use by protecting it from degradation.

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When does protein synthesis stop?

The process of protein synthesis ends when a stop codon enters the ribosome's A site, triggering events that lead to the release of the polypeptide chain and disassembly of the translation machinery.

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Study Notes

Course Information

  • Course: BMS 141
  • Lecture Number: 10 & 11
  • Title: Translation
  • Instructor: Dr. Lamees Dawood
  • Program: Medicine and Surgery
  • Semester: Fall 2024
  • University: Galala University

Intended Learning Outcomes

  • List components required for translation
  • Outline the mechanism of translation
  • Explain initiation steps of prokaryotic protein synthesis
  • Explain elongation steps of prokaryotic protein synthesis
  • Explain termination steps of prokaryotic protein synthesis
  • Identify post-translational modifications of polypeptide chains

Translation Components

  • Amino acids: All 20 amino acids needed.
  • Ribosomes: Large complexes of protein and rRNA.
  • tRNA: At least one per amino acid, some have more.
    • Prokaryotes typically use 70S ribosomes with subunits 30S and 50S, Eukaryotes use 80S ribosomes with subunits 40S and 60S
  • aminoacyl-tRNA synthetase: Enzymes to attach amino acids to tRNA.
  • Protein factors: Essential for initiation, elongation, and termination of protein synthesis
  • ATP & GTP: Energy sources for the process.
  • mRNA: Carries the genetic code.

Translation Process (Outline)

  • Initiation: mRNA binds to ribosome, initiation starts by binding to smaller subunit (30S in prokaryotes/40S in eukaryotes), followed by association of larger subunit (50S/60S) to form initiation complex.
    • The initiation complex consists of two ribosomal subunits, mRNA, initiator tRNA (methionine in eukaryotes, formyl-methionine in prokaryotes), GTP, and initiation factors.
    • Prokaryotes use IF-1, IF-2, and IF-3 as initiation factors; eukaryotes use over ten factors (eIFs). The 16S rRNA in Prokaryotic ribosomes recognizes the Shine-Dalgarno sequence in the mRNA. The 5' cap in eukaryotic mRNA is recognized by the ribosome and a complex of proteins, allowing translation to initiate.
  • Elongation: Adding amino acids to polypeptide chain
    • Three steps:
      • Binding of an incoming aminoacyl-tRNA
      • Peptide bond formation (Peptidyl transferase)
      • Translocation
  • Termination: Stop codon enters A site. Release factors recognize the stop codon. The peptide is released from the ribosome. The ribosomal subunits and mRNA are separated.

Overview of Protein Synthesis

  • mRNA carries the code, ribosome is the site of protein synthesis, tRNA brings amino acids to the ribosome, according to mRNA codons.

Post-Translational Modifications

  • Protein targeting (localization signals/sequences)
  • Protein folding
  • Trimming (removal of portions of a protein)
  • Covalent modification (e.g., phosphorylation, glycosylation, hydroxylation)
  • Protein degradation, using ubiquitination and proteasome.

Additional Information

  • Multiple ribosomes can translate the same mRNA simultaneously (polysomes).
  • Translation in prokaryotes and eukaryotes has differences (e.g., initiation factors).

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