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#ribosome recycling

2 public questions tagged with this topic.

Ribosome recycling in eukaryotes involves

Eukaryotes lack a direct RRF ortholog and utilize alternative surveillance and recycling machinery with different protein composition. Pelota, also called Dom34 in yeast, structurally resembles eRF1 and forms a complex with GTPase Hbs1, a relative of eRF3 and EF-Tu that recognizes stalled ribosomes and empty A-sites. Dom34-Hbs1 together with the ABC ATPase ABCE1, also called Rli1 in yeast, drives splitting of 80S into 40S and 60S subunits ATP-dependently. This pathway also participates in no-go decay and nonstop decay, clearing aberrant messages, differing mechanistically from bacterial RRF-EF

Ref: J Cell Biol 2012 Dom34-Hbs1-ABCE1 recycling complex; NCBI Review - eukaryotic ribosome recycling via Pelota-Hbs1-ABCE1

Ribosome recycling factor in prokaryotes is

Post-termination complexes contain deacylated tRNA and mRNA still bound to 70S ribosomes and require active disassembly for new elongation cycles. In bacteria, ribosome recycling factor RRF, a near-perfect tRNA shape mimic composed of helical bundle and domain resembling anticodon arm, binds to the A-site together with EF-G-GTP. GTP hydrolysis induces subunit rotation and splitting into 30S and 50S subunits, after which IF3 promotes tRNA dissociation and prevents reassociation, freeing subunits for initiation. EF-Tu functions only during elongation delivery, while eukaryotic homologs handle re

Ref: NCBI Bookshelf NBK21432 - RRF cooperates with EF-G to recycle ribosomes; Alberts Fig 6-81 ribosome recycling pathway