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Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping. It consists of four phases: initiation, elongation, termination, and recapping.
A ribosome is made up of two subunits, a small subunit, and a large subunit. These subunits come together before the translation of mRNA into a protein to provide a location for translation to be carried out and a polypeptide to be produced. [3] The choice of amino acid type to add is determined by a messenger RNA (mRNA) molecule. Each amino ...
[3] [4] The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a protein can be determined by methods such as Edman degradation or tandem mass spectrometry. Often, however, it is read directly from the sequence of the gene using the genetic code.
Some initiation factors, such as eIF4E, are important in synthesizing specific proteins needed for the proliferation and survival of cancer. [10] The careful selection of proteins ensures that proteins that are usually limited in translation and only proteins needed for cancer cell growth will be synthesized.
Structure of rabbit eIF3 in the context of the 43S PIC, showing subunits a, c, e, f, h, k, l, and m. [1]Eukaryotic initiation factor 3 (eIF3) is a multiprotein complex that functions during the initiation phase of eukaryotic translation. [2]
A bacterial initiation factor (IF) is a protein that stabilizes the initiation complex for polypeptide translation. Translation initiation is essential to protein synthesis and regulates mRNA translation fidelity and efficiency in bacteria. [1] The 30S ribosomal subunit, initiator tRNA, and mRNA form an initiation complex for elongation. [2]
The termination of translation requires coordination between release factor proteins, the mRNA sequence, and ribosomes. Once a termination codon is read, release factors RF-1, RF-2, and RF-3 contribute to the hydrolysis of the growing polypeptide, which terminates the chain. Bases downstream the stop codon affect the activity of these release ...
Poly(A)-binding protein is exported to the cytoplasm with the RNA. mRNAs that are not exported are degraded by the exosome. [39] [40] Poly(A)-binding protein also can bind to, and thus recruit, several proteins that affect translation, [39] one of these is initiation factor-4G, which in turn recruits the 40S ribosomal subunit. [41]