Protein translation and post-translational modification Flashcards Preview

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Flashcards in Protein translation and post-translational modification Deck (13)
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Draw the typical structure of mRNA

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What is the sequence for a start codon and what amino acid does it code for?

AUG and Methionine


Draw a diagram showing how an amino acid becomes attached to tRNA.? Include the name of the enzyme

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List the steps for Initiation

Step 1: dissociation of ribosome subunits (eukaryotic 40S + 60S)

Step 2: assembly of preinitiation complex containing Met-tRNA + eIFs + 40S subunit

Step 3: binding of mRNA to preinitiation complex

Step 4: binding of 60S subunit


Draw a diagram illustrating the steps for initiation

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List the steps for Elongation?

Step 1: binding of new tRNA carrying second amino acid to “amino acyl” (A) site

Step 2: catalysis of peptide bond formation between the two amino acids by peptidyl transferase (PT) on the large ribosomal subunit

Step 3: translocation of tRNA to P site and dissociation of first tRNA from E site


Name the 3 sites on a ribosome

E P A add pic


Draw a diagram illustrating the steps for Elongation

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List the steps for Termination

Step 1: recognition of stop codon Step 2: release of peptide chain Step 3: dissociation of release factors and ribosomes add pic


Explain why some antibiotics inhibit protein synthesis in prokaryotes but not in eukaryotes?

Translational machinery is complex, easily disrupted – common target for antibiotics Antibiotics exploit differences between prokaryotic and eukaryotic ribosomes and translation factors


What is a signal sequence?

First 20-24 amino acids = “signal sequence” (enriched in hydrophobic amino acids, e.g. Leu, Ile, Phe, Trp, Tyr, Ala)


Synthesis of proteins destined for the secretory pathway to the cell surface occurs on RER in the following stages: List these stages.

Step 1: Recognition of hydrophobic signal sequence by signal recognition particals (SRP)

Step 2: Binding of SRP to a receptor on the RER surface, translation resumes

Step 3: Translocation of growing peptide into the lumen of RER

Step 4: cleavage of signal sequence and protein folding

Transmembrance proteins have additional hydrophobic sequences that stick in the membrane of the RER

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Summarise the ways in which newly-synthesised proteins can be post-translationally modified

• Disulphide bond formation (e.g. insulin) • Proteolytic cleavage (e.g. insulin -> A and B chains) • Addition of carbohydrate (Glycosylation) • Addition of phosphate (Phosphorylation) • Addition of lipid groups (Prenylation, Acylation) • Hydroxylation (e.g. Collagen; Leitinger lecture)