أسئلة الثامنة جينتكس (قبل التعديل)

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Questions and Answers

What is co-translational modification in protein synthesis?

  • Activation of proteins through enzymatic action.
  • Chemical changes that happen while the protein is attached to the ribosome. (correct)
  • The removal of a peptide segment from an inactive protein.
  • Modifications that occur after protein synthesis is complete.

Which organelles are primarily involved in post-translational modifications?

  • Lysosomes and peroxisomes
  • Ribosomes and cytoplasm
  • Endoplasmic Reticulum and Golgi apparatus (correct)
  • Nucleus and mitochondria

What is a key function of chaperone proteins?

  • To enhance the speed of translation.
  • To assist in the proper folding of proteins. (correct)
  • To degrade misfolded proteins.
  • To modify proteins by adding lipid groups.

What process converts pre-proinsulin into insulin?

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

Which of the following modifications adds a phosphate group to a protein?

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

Which type of modification is responsible for adding a carboxylic group to a protein?

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

What is a possible consequence of protein misfolding?

<p>Development of diseases such as Alzheimer's (C)</p> Signup and view all the answers

What kind of modifications can proteins undergo via covalent modification?

<p>Attachment of various chemical groups (A)</p> Signup and view all the answers

What role does interferon play in the translational process?

<p>It stimulates phosphorylation of initiation factor 2 and inhibits translation. (C)</p> Signup and view all the answers

Which of the following substances inhibits protein synthesis by affecting elongation?

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

What is the function of protein phosphatases?

<p>Catalyze dephosphorylation of proteins. (C)</p> Signup and view all the answers

Which of the following processes is required for the maturation of collagen?

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

Heme influences protein synthesis by preventing what process?

<p>Phosphorylation of initiation factor 2 (B)</p> Signup and view all the answers

What impact does the carboxylation of proteins have in the human body?

<p>Is essential for clotting factors. (D)</p> Signup and view all the answers

Which mechanism of action of antibiotics is involved in the regulation of protein synthesis?

<p>Inhibition of protein synthesis at different stages. (D)</p> Signup and view all the answers

What is the primary consequence of diphtheria toxin's action on EF-2?

<p>Inhibition of translocation step leading to cell death. (C)</p> Signup and view all the answers

What is the primary site for post-translational modifications in cells?

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

Which of the following accurately describes the purpose of protein chaperones?

<p>To assist in protein folding (C)</p> Signup and view all the answers

What type of modification involves the addition of a hydroxyl group to amino acids in proteins?

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

Which condition can result from the abnormal folding of proteins?

<p>Alzheimer's disease (B)</p> Signup and view all the answers

What is one of the consequences of covalent modification of proteins?

<p>Activation or inactivation of proteins (D)</p> Signup and view all the answers

What role does glycosylation play in protein modification?

<p>Adds carbohydrate groups to proteins (A)</p> Signup and view all the answers

Which process refers to the removal of part of the peptide chain from a protein?

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

Phosphorylation of proteins is particularly significant for which purpose?

<p>Regulating protein activity (A)</p> Signup and view all the answers

What effect does interferon have on the translational process?

<p>It inhibits IF-2 phosphorylation. (D)</p> Signup and view all the answers

Which enzyme is responsible for catalyzing the dephosphorylation of proteins?

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

What is the primary function of diphtheria toxin in the context of protein synthesis?

<p>It inhibits elongation factor 2. (C)</p> Signup and view all the answers

How does heme influence globin synthesis?

<p>By inhibiting IF-2 phosphorylation. (D)</p> Signup and view all the answers

What role do protein kinases play in the regulation of translation?

<p>They catalyze phosphorylation processes. (D)</p> Signup and view all the answers

Which of the following statements accurately describes the effect of antibiotics on protein synthesis?

<p>They inhibit protein synthesis at different stages. (A)</p> Signup and view all the answers

What does the carboxylation of proteins contribute to in the human body?

<p>Maturation of blood clotting factors. (D)</p> Signup and view all the answers

Which aspect of protein synthesis is primarily controlled at the initiation stage?

<p>Activity of initiation factors. (D)</p> Signup and view all the answers

What are the two main types of modifications that proteins undergo post-translationally?

<p>Co-translational and post-translational modifications.</p> Signup and view all the answers

Why do some proteins require chaperones for proper folding?

<p>Some proteins do not fold spontaneously and need chaperones to achieve their correct functional shape.</p> Signup and view all the answers

Give an example of a protein that undergoes trimming in post-translational processing.

<p>Pre-Proinsulin is converted into insulin.</p> Signup and view all the answers

What modifications can occur through covalent modification of proteins?

<p>Phosphorylation, hydroxylation, carboxylation, and glycosylation.</p> Signup and view all the answers

How does phosphorylation affect the activity of proteins?

<p>Phosphorylation typically activates or modifies the function of proteins.</p> Signup and view all the answers

What is the significance of glycosylation in protein function?

<p>Glycosylation influences protein folding, stability, and cell recognition.</p> Signup and view all the answers

What is one consequence of protein abnormal folding?

<p>One consequence is the development of diseases such as Alzheimer's disease.</p> Signup and view all the answers

Describe the role of the endoplasmic reticulum in post-translational modifications.

<p>The endoplasmic reticulum is involved in folding proteins and initiating modifications.</p> Signup and view all the answers

How does phosphorylation by protein kinases influence cellular processes?

<p>Phosphorylation by protein kinases can activate or deactivate proteins, thereby regulating various cellular processes including cell growth and metabolism.</p> Signup and view all the answers

What is the role of protein phosphatases in cellular functions?

<p>Protein phosphatases catalyze the dephosphorylation of proteins, reversing the effects of protein kinases and thus playing a vital role in signaling pathways.</p> Signup and view all the answers

In what way does heme affect the synthesis of globin?

<p>Heme stimulates globin synthesis by inhibiting the phosphorylation of initiation factor IF-2, promoting the translation process.</p> Signup and view all the answers

Describe the impact of diphtheria toxin on protein synthesis.

<p>Diphtheria toxin inhibits elongation factor EF-2, preventing the translocation step in protein synthesis, which can lead to cell death.</p> Signup and view all the answers

How does interferon modulate protein synthesis at the initiation level?

<p>Interferon stimulates the phosphorylation of initiation factor IF-2, which inhibits translation and decreases viral protein synthesis.</p> Signup and view all the answers

What is the consequence of carboxylation in the maturation of proteins?

<p>Carboxylation is essential for the maturation of proteins like clotting factors, affecting their functional capabilities.</p> Signup and view all the answers

Explain the role of glycosylation in protein modification.

<p>Glycosylation involves the addition of carbohydrate groups to proteins, influencing their stability, localization, and activity.</p> Signup and view all the answers

What is the significance of controlling the translational process in response to viral infections?

<p>Controlling the translational process helps cells limit viral protein synthesis, thereby inhibiting viral replication.</p> Signup and view all the answers

How do protein kinases specifically influence protein function?

<p>Protein kinases add phosphate groups to proteins, thus modifying their activity and function.</p> Signup and view all the answers

Discuss the effect of interferon on viral protein synthesis.

<p>Interferon stimulates phosphorylation of IF-2, inhibiting translation and decreasing viral protein synthesis.</p> Signup and view all the answers

What is the role of EF-2 in protein synthesis, and how does diphtheria toxin affect it?

<p>EF-2 is essential for the translocation step in elongation; diphtheria toxin inhibits EF-2, stopping protein synthesis.</p> Signup and view all the answers

Explain the significance of carboxylation in the maturation of proteins.

<p>Carboxylation is necessary for the activation of certain proteins, such as clotting factors involved in coagulation.</p> Signup and view all the answers

How does heme interact with the synthesis of globin at a translational level?

<p>Heme prevents phosphorylation of IF-2, thus promoting globin synthesis by enhancing translation initiation.</p> Signup and view all the answers

What mechanism explains the action of antibiotics on bacterial protein synthesis?

<p>Antibiotics inhibit protein synthesis by targeting specific stages of translation in bacteria.</p> Signup and view all the answers

In what way do protein phosphatases counter the action of protein kinases?

<p>Protein phosphatases remove phosphate groups from proteins, reversing the effects of phosphorylation.</p> Signup and view all the answers

Describe how post-translational modifications can impact the pathophysiology of diseases.

<p>Alterations in post-translational modifications can lead to misfolded proteins and contribute to various diseases.</p> Signup and view all the answers

What role do chaperones play in protein folding, and why might certain proteins require them?

<p>Chaperones assist in the proper folding of proteins, helping prevent misfolding that can lead to diseases. Some proteins require them because they cannot fold correctly on their own due to their complex structures.</p> Signup and view all the answers

Describe the process of trimming in post-translational modifications and give an example.

<p>Trimming involves the removal of segments from the peptide chain to convert inactive proteins into their active forms. An example is the conversion of pre-proinsulin into insulin.</p> Signup and view all the answers

Why is phosphorylation considered a significant post-translational modification, and what effect does it have on proteins?

<p>Phosphorylation adds a phosphate group to proteins, which can activate or deactivate their functions. It plays a crucial role in regulating enzymatic activity and signaling pathways.</p> Signup and view all the answers

What is glycosylation, and how does it impact protein function?

<p>Glycosylation is the addition of carbohydrate groups to proteins, affecting stability, localization, and recognition by other molecules. It is vital for proper protein functioning and interactions.</p> Signup and view all the answers

Explain the significance of correctly folded proteins in relation to diseases such as Alzheimer's.

<p>Correctly folded proteins are essential for normal cellular function, while misfolded proteins can aggregate and lead to diseases like Alzheimer's. These aggregates disrupt cellular processes and promote neurodegeneration.</p> Signup and view all the answers

What are covalent modifications, and how do they influence protein activity?

<p>Covalent modifications involve chemical changes to amino acid residues, affecting a protein's structure and function. These modifications can either activate or inactivate proteins, impacting various biological pathways.</p> Signup and view all the answers

Discuss the impact of improper post-translational modifications on protein stability.

<p>Improper post-translational modifications can lead to instability and a loss of function in proteins, potentially resulting in aggregation and cellular damage. This instability can trigger various diseases.</p> Signup and view all the answers

In what way do the endoplasmic reticulum and Golgi apparatus collaborate during post-translational processing?

<p>The endoplasmic reticulum facilitates initial folding and modifications of new proteins, while the Golgi apparatus further processes and sorts these proteins for their final destination. Together, they ensure proteins are correctly modified and functional.</p> Signup and view all the answers

Flashcards

Post-translational modifications

Chemical modifications of a protein after its synthesis.

Protein folding

Polypeptide chain acquiring its 3D structure to function properly.

Protein trimming

Removing parts of a polypeptide chain.

Zymogen activation

Converting an inactive protein (zymogen) into an active one.

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Covalent modification

Attaching chemical groups to amino acids for altering protein activity.

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Phosphorylation

Adding a phosphate group to a protein.

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Hydroxylation

Adding a hydroxyl group to a protein.

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Carboxylation

Adding a carboxylic acid group to a protein.

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Glycosylation

Adding a carbohydrate (CHO) group to a protein.

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Protein Chaperones

Assist in protein folding processes.

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Protein Phosphorylation

The addition of a phosphate group to a protein, altering its activity.

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Protein Hydroxylation

Adding a hydroxyl group to a protein; important for collagen maturation.

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Protein Carboxylation

Adding a carboxyl group to a protein; crucial for clotting factors.

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Protein Glycosylation

Attaching carbohydrate chains to a protein; crucial for protein function & structure.

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Protein kinases

Enzymes that catalyze protein phosphorylation.

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Protein phosphatases

Enzymes that catalyze protein dephosphorylation.

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Initiation Factors (IF-2)

Proteins that control the initiation of protein synthesis.

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Elongation Factor 2 (EF-2)

Protein necessary for elongation step in protein synthesis.

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Post-translational Processing

Modifications to proteins after their synthesis, affecting their function.

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Regulation of Translation

Controlling the rate at which proteins are made.

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Post-translational processing

Chemical changes to a protein after it's made.

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Protein folding

Protein chains folding into their 3D shape.

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Protein trimming

Removing parts of a protein chain.

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Zymogen activation

Turning an inactive protein into an active one.

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Covalent modification

Adding chemical groups to alter the protein.

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Phosphorylation

Adding a phosphate group to a protein.

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Hydroxylation

Adding a hydroxyl group to a protein.

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Carboxylation

Adding a carboxyl group to a protein.

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Glycosylation

Adding sugars to a protein.

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Protein Chaperones

Help proteins fold correctly.

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Protein Kinases

Enzymes that add phosphate groups to proteins, altering their activity.

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Protein Phosphatases

Enzymes that remove phosphate groups from proteins, altering their activity.

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IF-2

Protein initiating protein creation, its activity can be controlled.

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EF-2

Protein required for elongation stage of protein synthesis.

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Translation Regulation

Controlling the speed at which proteins are made

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Protein Hydroxylation

Adding a hydroxyl group to a protein. Important for collagen.

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Protein Carboxylation

Adding a carboxyl group to a protein affecting factors like clotting.

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Protein Glycosylation

Adding a carbohydrate to a protein (CHO), essential for function and design

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Post-translational Processing

Chemical modifications that happen to a protein after it's made.

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Protein Folding

Protein chains arranging themselves into 3D shapes needed to function.

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Protein Trimming

Removing parts of a protein chain after its creation.

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Zymogen Activation

Turning an inactive protein into an active one.

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Covalent Modification

Adding chemical groups to protein amino acids to alter protein activity

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Phosphorylation

Adding a phosphate group to a protein to change its activity.

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Hydroxylation

Adding a hydroxyl group to a protein.

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Carboxylation

Adding a carboxyl group to a protein.

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Glycosylation

Attaching a carbohydrate chain to a protein.

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Protein Kinases

Enzymes that add phosphate groups to proteins, changing their activity.

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Protein Phosphatases

Enzymes that remove phosphate groups from proteins, changing their activity.

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IF-2

A protein initiating protein synthesis, its activity can be regulated.

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EF-2

Protein necessary for the elongation step in protein synthesis.

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Translation Regulation

Controlling the rate at which proteins are made

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Protein Hydroxylation

Adding a hydroxyl group to a protein; important for collagen maturation.

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Carboxylation of Protein

Adding a carboxyl group to a protein, crucial for clotting factors.

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Protein Glycosylation

Attaching carbohydrates (CHO) to a protein, vital for protein function and structure.

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Post-translational Processing

Chemical modifications to a protein after its initial synthesis; affects its function.

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Post-translational Processing

Chemical modifications that happen to a protein after it is made, affecting its function.

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Protein Folding

Protein chains arranging themselves into 3D shapes needed for function.

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Protein Trimming

Removing parts of a protein chain after its creation.

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Zymogen Activation

Turning an inactive protein (zymogen) into an active one.

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Covalent Modification

Adding chemical groups to protein amino acids to alter protein activity.

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Phosphorylation

Adding a phosphate group to a protein to change its activity.

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Hydroxylation

Adding a hydroxyl group to a protein.

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Carboxylation

Adding a carboxyl group to a protein.

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Glycosylation

Attaching a carbohydrate chain to a protein.

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Protein Kinases

Enzymes that add phosphate groups to proteins, changing their activity

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Protein Phosphatases

Enzymes that remove phosphate groups from proteins

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IF-2

Protein that initiates protein synthesis, its activity is adjustable.

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EF-2

Protein required for protein synthesis elongation.

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Translation Regulation

Controlling protein production speed

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Protein Hydroxylation

Adding a hydroxyl group to a protein. Important for collagen.

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Protein Carboxylation

Adding a carboxyl group to a protein, often for clotting.

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Protein Glycosylation

Attaching a carbohydrate to a protein. Crucial for protein structure and function.

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Post-translational Processing

Chemical modifications to a protein after its creation. Affects the protein's action.

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Protein Folding

Protein chains arranging into 3-D shapes needed to work.

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Study Notes

Protein Modifications (Processing)

  • Protein modifications occur either co-translationally (while attached to ribosome) or post-translationally (after synthesis).
  • Post-translational processing modifies polypeptides or amino acid residues after protein synthesis.
  • The modifications occur in endoplasmic reticulum and Golgi apparatus.
  • Protein folding is crucial for protein function.
  • Secondary, tertiary, and quaternary structures are formed through folding.
  • Some proteins need chaperones to fold correctly.
  • Improper folding can lead to diseases like Alzheimer's.

Protein Trimming

  • Trimming involves removing parts of the peptide chain.
  • This process converts inactive proteins to active forms.
  • Examples include pre-proinsulin converting to insulin and inactive pancreatic trypsinogen becoming active trypsin.
  • Proteins may be activated or inactivated by adding chemical groups to their amino acids.

Covalent Modification

  • Chemical groups are attached covalently to the protein.
  • Examples include phosphorylation, hydroxylation, carboxylation, and glycosylation.
  • Phosphorylation adds a phosphate group.
  • Hydroxylation adds a hydroxyl group to proline.
  • Carboxylation adds a carboxyl group to glutamate.
  • Glycosylation adds a carbohydrate group.

Regulation of Translation

  • Translation process is regulated by initiation factors (IF-2).
  • Interferon (anti-viral drug) stimulates IF-2 phosphorylation, inhibiting viral replication.
  • Heme increases globin synthesis by preventing IF-2 phosphorylation.
  • Diphtheria toxin inhibits elongation factor 2 (EF-2), inhibiting protein synthesis.

Clinical Correlates

  • Some drugs affect protein synthesis rate.
  • Interferon stimulates IF-2 phosphorylation, decreasing viral protein synthesis.
  • Antibiotics can inhibit protein synthesis at various stages within bacterial cells.
  • Diphtheria toxin inhibits EF-2, preventing translocation, and causing cell death.

Translation Inhibitors (Antibiotics)

  • Antibiotics target bacterial protein synthesis.
  • Streptomycin interferes with initiation or misreads mRNA.
  • Tetracycline blocks the A site, preventing aminoacyl-tRNA binding.
  • Erythromycin inhibits translocation.
  • Puromycin causes premature termination.

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