Short answers, pulled from the story.
Translation is the process by which cells build proteins using messenger RNA as a template. Ribosomes read the mRNA in three-nucleotide units called codons, each specifying one amino acid. Without translation, no proteins could be made, and no cellular function could proceed.
The four stages are initiation, elongation, termination, and recycling. Initiation assembles the ribosome at the start codon on the mRNA. Elongation adds amino acids one at a time. Termination releases the finished polypeptide when a stop codon is reached. Recycling breaks apart the ribosome subunits for reuse.
Prokaryotic ribosomes incorporate up to 17 to 21 amino acid residues per second, roughly three times faster than eukaryotic ribosomes, which add up to 6 to 9 residues per second. The difference reflects structural and regulatory distinctions between the two ribosome types.
Several antibiotics, including chloramphenicol, tetracycline, streptomycin, erythromycin, and puromycin, target bacterial ribosomes to block translation. Prokaryotic ribosomes have a different structure from eukaryotic ribosomes, allowing these drugs to disable bacterial protein synthesis without harming human cells.
Functional translational readthrough occurs in a small number of human genes where the RNA sequence near a stop codon makes termination inefficient, allowing up to 10% of ribosomes to read past the stop codon. In some of these genes, the extended sequence encodes a functional protein domain, producing a distinct protein isoform.
Cancer cells reprogram translation through major oncogenic signaling pathways, including RAS-MAPK, PI3K/AKT/mTOR, MYC, and WNT-beta-catenin. Rather than genetically altering translation factors, cancer cells more commonly adjust the levels of existing ones. During metabolic stress, cancer cells also translate survival mRNAs, such as those activating AMPK, to escape programmed cell death.