Translation

Protein translation enables the conversion of the genetic information encoded in mRNA (messenger RNA) into functional proteins required by cells. This process involves a series of coordinated steps, each with its own key features. Ribosomes are the structures responsible for protein translation. They consist of the large and small ribosomal subunits, each composed of ribosomal RNA (rRNA) and ribosomal proteins. In vertebrates, ribosomes are present in the cytoplasm and on the endoplasmic reticulum (ER), depending on the destination of the translated protein. Ribosomes catalyse the synthesis of proteins by firstly facilitating the base pairing of aminoacyl-tRNA molecules to the mRNA template and then catalysing peptide bond formation between amino acids. The genetic code comprises a set of three nucleotide codons, with 64 possible codons, including the start codon (AUG) and three stop codons (UAA, UAG, and UGA) encoding the twenty standard amino acids. Transfer RNA (tRNA) molecules, each with a specific anticodon, first bring amino acids to the ribosome. The tRNA anticodon base-pairs with the complementary mRNA codon, ensuring the correct amino acid incorporates into the growing polypeptide chain. Protein translation begins with the recognition of the start codon (AUG) by the small ribosomal subunit, facilitated by initiation factors. In vertebrates, the start codon is typically preceded by the 5' cap structure. The initiator tRNA carrying methionine (tRNAiMet) binds to the start codon, and the large ribosomal subunit joins forming the complete ribosome. During peptide elongation, aminoacyl-tRNA molecules, guided by the mRNA codons and tRNA anticodons, enter the ribosomal A site, one of the three binding sites within the ribosome, and undergoes peptidyl transferase catalysis, the formation of a peptide bond between the amino acid carried by the A-site tRNA and the growing polypeptide chain attached to the tRNA in the P (peptidyl) site. After the peptide bond is formed, the ribosome undergoes a process called translocation. During translocation, the ribosome moves one codon along the mRNA strand, shifting the A site tRNA (now carrying the dipeptide) to the P site and making the A site available for the next aminoacyl-tRNA to bind. This process continues iteratively, with each new amino acid added to the growing polypeptide chain. When a stop codon (UAA, UAG, or UGA) enters the A site, protein translation is terminated. Unlike regular amino acids, there are no tRNA molecules that recognize stop codons. Release factors (e.g., eRF1 and eRF3 in vertebrates) bind to the ribosome in response to a stop codon, triggering the release of the completed polypeptide chain from the ribosome. Newly synthesized polypeptides undergo complex folding events, often assisted by chaperone proteins, to achieve their functional conformations. In vertebrates, many secretory and membrane proteins are also co-translationally targeted to the endoplasmic reticulum (ER), with the Signal recognition particle (SRP) recognizing a signal peptide on the nascent polypeptide and directing the ribosome-mRNA complex to the ER membrane. Vertebrates additionally have a surveillance mechanism called NMD that detects and degrades mRNAs containing premature stop codons, thereby preventing the synthesis of truncated, non-functional proteins. We provide a large product range of research reagents for investigating protein translation, including eIF4EBP1 antibodies, Nucleophosmin antibodies, Nucleolin antibodies, Angiogenin ELISA Kits, and eIF4EBP1 ELISA Kits. Explore our full protein translation product range below and discover more, for less. Alternatively, you can explore our Ribosome, Regulation, and Mitochondria Translation product ranges.