Translation and Post-Translational Modification (1B) - Bio & Biochem
- What are the three stop codons in the standard genetic code?
- UAA, UAG, UGA. These codons do not code for amino acids but signal the end of translation by binding release factors.
- What is the Shine-Dalgarno sequence used for in prokaryotic translation initiation?
- Aligns mRNA on the subunit via rRNA pairing. The Shine-Dalgarno sequence base-pairs with 16S rRNA to position the start codon correctly in the P site.
- What is the role of chaperone proteins in post-translational processing?
- Assist folding and prevent aggregation without changing sequence. Chaperones bind nascent polypeptides to promote proper folding and inhibit misfolding or aggregation without altering the amino acid sequence.
- What is the role of the poly(A) tail in eukaryotic translation efficiency?
- Enhances translation and stabilizes mRNA via PABP interactions. The poly(A) tail binds poly(A)-binding proteins, which interact with initiation factors to circularize mRNA and promote reinitiation.
- Which cellular compartment is the primary site of translation for secreted proteins?
- Rough endoplasmic reticulum (RER)-bound ribosomes. Secreted proteins have signal sequences that direct ribosomes to the RER for co-translational translocation into the ER lumen.
- What enzyme activity in the large ribosomal subunit forms peptide bonds?
- Peptidyl transferase (rRNA ribozyme activity). This ribosomal RNA catalyzes the formation of peptide bonds between amino acids during elongation.
- What is the immediate energetic cost to add one amino acid during elongation (high-energy bonds)?
- high-energy bonds (ATPAMP counts as ) plus GTP. Charging tRNA hydrolyzes ATP to AMP (two bonds), and elongation requires two GTP for tRNA delivery and translocation.
- Identify the eukaryotic mRNA feature required for cap-dependent ribosome recruitment.
- mRNA cap (mG cap). The 5' cap recruits initiation factors and the 40S subunit, enabling scanning for the start codon.
- Which post-translational modification commonly regulates enzyme activity by adding a phosphate group?
- Phosphorylation of Ser/Thr/Tyr residues. Phosphorylation adds phosphate groups to specific residues, modulating protein function, activity, or localization through conformational changes.
- Which factor and nucleotide deliver aminoacyl-tRNA to the A site in eukaryotes?
- eEF1A with GTP. eEF1A-GTP forms a ternary complex with aminoacyl-tRNA, ensuring accurate delivery and proofreading at the A site.
- Which ribosomal site holds the tRNA carrying the growing polypeptide chain?
- P site. The P site secures the tRNA with the nascent chain, positioning it for transfer to the incoming amino acid.
- Which process allows one mRNA to be translated by multiple ribosomes simultaneously?
- Polysome (polyribosome) formation. Polysomes increase protein synthesis efficiency by allowing concurrent translation of a single mRNA by multiple ribosomes.
- What is the key difference between prokaryotic and eukaryotic ribosomes by subunits?
- Prokaryotic ; eukaryotic . Prokaryotic and eukaryotic ribosomes differ in size and subunit composition, reflecting evolutionary divergence.
- Which molecule recognizes stop codons and terminates translation?
- Release factor (RF/eRF). Release factors mimic tRNA to bind stop codons, triggering hydrolysis and polypeptide release from the ribosome.
- What is ubiquitination, and what is its most common consequence for a protein?
- Covalent ubiquitin tagging; targets protein for proteasomal degradation. Ubiquitination marks proteins for degradation by attaching ubiquitin chains, recognized by the proteasome for proteolysis.
- What is the start codon for translation, and which amino acid does it encode?
- AUG; methionine (Met) (fMet in bacteria). AUG initiates translation by recruiting the initiator tRNA, specifying methionine as the first residue in the polypeptide.
- What is the Kozak sequence used for in eukaryotic translation initiation?
- Consensus around AUG that promotes start site recognition. The Kozak sequence optimizes initiation by enhancing ribosome binding and scanning efficiency around the AUG codon.
- Which factor and nucleotide drive ribosomal translocation during elongation in eukaryotes?
- eEF2 with GTP. eEF2-GTP hydrolysis powers the movement of the ribosome along mRNA by one codon during elongation.
- Which ribosomal site binds the incoming aminoacyl-tRNA during elongation?
- A site. The A site accommodates the next charged tRNA, allowing codon-anticodon pairing and peptide bond formation.
- Which ribosomal site holds the deacylated tRNA just before it exits the ribosome?
- E site. The E site temporarily holds the empty tRNA after peptide transfer, facilitating its release from the ribosome.
- What is the function of aminoacyl-tRNA synthetase in translation?
- Charges tRNA with its correct amino acid using ATP. This enzyme ensures accurate amino acid attachment to tRNA, enabling proper codon recognition during protein synthesis.
- What is the direction of mRNA translation by the ribosome?
- mRNA is read . Ribosomes decode mRNA in the 5' to 3' direction to match the synthesis polarity of nucleic acids.
- What post-translational modification forms disulfide bonds, and where does it usually occur?
- Disulfide bond formation; typically in ER lumen (oxidizing environment). Disulfide bonds stabilize protein structure through cysteine oxidation, occurring in the ER due to its oxidizing conditions.
- What is the function of the signal recognition particle (SRP) in protein targeting?
- Binds signal peptide, pauses translation, targets ribosome to RER. SRP recognizes the N-terminal signal peptide, halts elongation, and docks the ribosome to the ER translocon for protein insertion.