The assembly factor Reh1 is released from the ribosome during its initial round of translation DOI Creative Commons
Sharmishtha Musalgaonkar, James N. Yelland, Ruta Chitale

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: Feb. 3, 2025

Assembly of functional ribosomal subunits and successfully delivering them to the translating pool is a prerequisite for protein synthesis cell growth. In S. cerevisiae, ribosome assembly factor Reh1 binds pre-60S at late stage during their cytoplasmic maturation. Previous work shows that C-terminus inserts into polypeptide exit tunnel subunit. Here, we show Reh1-bound nascent 60S associate with 40S form actively ribosomes. Using selective profiling, found ribosomes populate open reading frames near start codons. are also strongly enriched initiator tRNA, indicating they associated early elongation. cryo-electron microscopy image 80S ribosomes, contain A site peptidyl P tRNA eIF5A, does not dissociate from until translation We propose displaced by elongating peptide chain, making it last released subunit its initial round translation. aided dedicated factors. authors positioned in suggesting growing chain displaces first

Language: Английский

The assembly factor Reh1 is released from the ribosome during its initial round of translation DOI Creative Commons
Sharmishtha Musalgaonkar, James N. Yelland, Ruta Chitale

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: Feb. 3, 2025

Assembly of functional ribosomal subunits and successfully delivering them to the translating pool is a prerequisite for protein synthesis cell growth. In S. cerevisiae, ribosome assembly factor Reh1 binds pre-60S at late stage during their cytoplasmic maturation. Previous work shows that C-terminus inserts into polypeptide exit tunnel subunit. Here, we show Reh1-bound nascent 60S associate with 40S form actively ribosomes. Using selective profiling, found ribosomes populate open reading frames near start codons. are also strongly enriched initiator tRNA, indicating they associated early elongation. cryo-electron microscopy image 80S ribosomes, contain A site peptidyl P tRNA eIF5A, does not dissociate from until translation We propose displaced by elongating peptide chain, making it last released subunit its initial round translation. aided dedicated factors. authors positioned in suggesting growing chain displaces first

Language: Английский

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