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Most eukaryotic cellular mRNAs are blocked at their 5'-ends with the 7-methyl-guanosine five-prime cap structure, m7GpppX (where X is any nucleotide). This structure is involved in several cellular processes including enhanced translational efficiency, splicing, mRNA stability, and RNA nuclear export. eIF4E is a eukaryotic translation initiation factor involved in directing ribosomes to the ...
The prokaryotic initiation factor, IF3, assists with start site specificity, as well as mRNA binding. [2] [3] This is in comparison with the eukaryotic initiation factor, eIF1, who also performs these functions. The elF1 structure is similar to the C-terminal domain of IF3, as they each contain a five-stranded beta sheet against two alpha ...
Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation .
In molecular biology, the eukaryotic translation initiation factor 4E family (eIF-4E) is a family of proteins that bind to the cap structure of eukaryotic cellular mRNAs. [1] Members of this family recognise and bind the 7-methyl- guanosine -containing (m7Gppp) cap during an early step in the initiation of protein synthesis and facilitate ...
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.
Eukaryotic translation initiation factor 4E-binding protein 1 (also known as 4E-BP1) is a protein that in humans is encoded by the EIF4EBP1 gene. [5] inhibits cap-dependent translation by binding to translation initiation factor eIF4E. Phosphorylation of 4E-BP1 results in its release from eIF4E, thereby allows cap-dependent translation to ...
While prokaryotes are able to undergo both cellular processes simultaneously, the spatial separation that is provided by the nuclear membrane prevents this coupling in eukaryotes. Eukaryotic elongation factor 2 (eEF2) is a regulateable GTP-dependent translocase that moves nascent polypeptide chains from the A-site to the P-site in the ribosome.
Eukaryotic ribosomes are known to bind to transcripts in a mechanism unlike the one involving the 5' cap, at a sequence called the internal ribosome entry site. This process is not dependent on the full set of translation initiation factors (although this depends on the specific IRES) and is commonly found in the translation of viral mRNA. [9]