tRNAs, the Genetic Code, and Translation in General Biology
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A codon is a 3-letter sequence of mRNA read 5’ to 3’ that corresponds to one amino acid or a stop signal during translation.
The start codon is 5’AUG3’ and it codes for methionine, which is the first amino acid in protein synthesis.
The stop codons are 5’UAA3’, 5’UGA3’, and 5’UAG3’. They signal termination of translation.
The anticodon is a 3-nucleotide sequence on tRNA that pairs antiparallel and complementary to the mRNA codon during translation.
tRNA folds into a complex secondary structure stabilized by intramolecular hydrogen bonds (base pairing within the same molecule).
The 5’CCA3’ sequence at the amino acid end of tRNA is added after transcription and is the site where the amino acid attaches.
Aminoacyl-tRNA synthetases charge tRNAs by attaching the correct amino acid to its corresponding tRNA using ATP.
The wobble base pairing allows flexibility in pairing between the 5’ anticodon position of tRNA and the 3’ codon position of mRNA, enabling one tRNA to recognize multiple codons.
Inosine (I) in the 5’ position of the anticodon can pair with U, C, or A in the codon, increasing codon recognition flexibility.
There are 6 possible reading frames in double-stranded DNA: 3 on each strand read 5’ to 3’.
An ORF is a sequence from a start codon to an in-frame stop codon that potentially encodes a protein.
The 5’ UTR contains regulatory sequences that help ribosomes bind and initiate translation at the correct start codon.
The ribosome binding site is part of the 5’ UTR and aligns the start codon with the ribosome's P site for translation initiation.
The three phases are initiation, elongation, and termination.
The energy comes from the high-energy bond between the amino acid and tRNA formed during charging, not from GTP hydrolysis.
Tetracycline blocks the A site of bacterial ribosomes, preventing elongation by stopping aminoacyl-tRNA entry.
Ricin removes a specific adenine from ribosomal RNA in the large subunit, halting protein synthesis and killing the cell.
Bound ribosomes are attached to the ER and translate membrane or secreted proteins; free ribosomes translate cytosolic proteins. Ribosomes can switch based on signal sequences.
Release factors recognize stop codons and promote termination by releasing the newly made polypeptide from the ribosome.
By blocking new protein synthesis with a ribosome poison and measuring protein levels over time (e.g., via Western blot), the natural degradation rate (half-life) can be determined.