The arrival of any of the three stop codons (UAA, UAG and UGA) into the ribosomal A-site triggers the binding of a release factor (RF) to the ribosome and subsequent polypeptide chain release. In eukaryotes, the RF is composed of two proteins, eRF1 and eRF3. eRF1 is responsible for the hydrolysis of the peptidyl-tRNA, while eRF3 provides a GTP-dependent function. The ribosome releases the mRNA and dissociates into its two complex subunits, which can reassemble on another molecule to begin a new round of protein synthesis. It should be noted that at present, there is no factor identified in eukaryotes that would be the functional equivalent of the bacterial ribosome release (or recycling) factor, RRF, that catalyzes dissociation of the ribosome from the mRNA following release of the polypeptide
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Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T.; ''The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein.''; PubMedEurope PMCScholia
Frolova L, Le Goff X, Rasmussen HH, Cheperegin S, Drugeon G, Kress M, Arman I, Haenni AL, Celis JE, Philippe M.; ''A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor.''; PubMedEurope PMCScholia
Salas-Marco J, Bedwell DM.; ''GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination.''; PubMedEurope PMCScholia
Jones WM, Scaloni A, Bossa F, Popowicz AM, Schneewind O, Manning JM.; ''Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities.''; PubMedEurope PMCScholia
Erlandsson R, Boldog F, Persson B, Zabarovsky ER, Allikmets RL, Sümegi J, Klein G, Jörnvall H.; ''The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase.''; PubMedEurope PMCScholia
Figaro S, Scrima N, Buckingham RH, Heurgué-Hamard V.; ''HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1.''; PubMedEurope PMCScholia
Hoshino S, Imai M, Mizutani M, Kikuchi Y, Hanaoka F, Ui M, Katada T.; ''Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1.''; PubMedEurope PMCScholia
Ichikawa S, Kaji A.; ''Molecular cloning and expression of ribosome releasing factor.''; PubMedEurope PMCScholia
Protein acetylation, which can occur during or after polypeptide chain biosynthesis, helps protect the intracellular proteins from proteolysis. Acylamino-acid-releasing enzyme (APEH) is a cytosolic enzyme able to catalyse the preferential hydrolysis of terminal acetylated amino acids from small acetylated peptides. APEH prefers substrates with acetylated methionine, alanine and serine residues. Hydrolysis produces an acetylated amino acid and a N-terminus protein (Jones et al. 1991). APEH expression is reduced in renal cell carcinoma therefore may represent a tumor suppressor gene, whose loss contributes to the development of renal cell carcinoma (Erlandsson et al. 1991). The hydrolysis of an acetylated serine residue (NAc-Ser-protein) is shown here.
Class 1 release factors such as eukaryotic peptide chain release factor subunit 1 (ETF1) direct the termination of peptide translation in response to the termination codons UAA, UAG and UGA. ETF1 needs to be complexed with ERF3 in its GTP-bound form to be efficiently post-translationally methylated. HemK methyltransferase family member 2 (N6AMT1) is a heterodimeric methyltransferase that catalyses N5-methylation of ETF1 on glutamine 185 (Q185), using S-adenosyl L-methionine (AdoMet) as the methyl donor (Figaro et al. 2008). N6AMT1 forms a complex with multifunctional methyltransferase subunit TRM112-like protein (TRMT112)
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DataNodes
dimer:GSPT2:GDP:80S
Ribosome:mRNA:peptidyl-tRNA Complexdimer:GSPT2:GDP:80S Ribosome:mRNA:tRNA
Complexdimer:GSPT2:GTP:80S
Ribosome:mRNA:peptidyl-tRNAAnnotated Interactions
dimer:GSPT2:GDP:80S
Ribosome:mRNA:peptidyl-tRNA Complexdimer:GSPT2:GDP:80S
Ribosome:mRNA:peptidyl-tRNA Complexdimer:GSPT2:GDP:80S Ribosome:mRNA:tRNA
Complexdimer:GSPT2:GTP:80S
Ribosome:mRNA:peptidyl-tRNAdimer:GSPT2:GTP:80S
Ribosome:mRNA:peptidyl-tRNA