Authors
Xiaoyun Yang, Zongqiang Li, Qiang He, Yangkai Zhou, Chuanlun Zhang, Senfang Sui
Published in
Science China. Life sciences. Oct 08, 2026. Epub Oct 08, 2026.
Abstract
Ribosome, the universally conserved cellular machinery, orchestrates protein synthesis across all organisms. Ribosome-associated factors that regulate translation during biogenesis and stress adaptation remain underexplored in archaea due to limited structural data. Here we present eight cryogenic electron microscopy (cryo-EM) structures of the archaeal 50S ribosomal subunit at resolutions of 2.07-3.26 Å, revealing a previously uncharacterized cystathionine β-synthase (CBS) domain-containing protein positioned above the peptidyl transferase center, with an extended loop that inserts deeply into the peptide exit tunnel. Intriguingly, distinct adenosine derivatives occupy the ligand-binding pocket of the CBS protein in different structural states of the 50S subunit. Molecular dynamics simulations indicate that ATP binding induces a more contracted conformation of the extended loop, suggesting that nucleotide occupancy may modulate this protein's ribosome-association mode. Biochemical and bioinformatic analyses reveal that the extended loop is predominantly found in archaea, suggesting lineage-specific adaptations of ribosome-associated CBS proteins. Furthermore, the relatively sparse and dispersed distribution of rRNA modifications likely reflects organism-specific adaptations. Collectively, this work provides a structural framework for understanding how CBS-family proteins engage the archaeal ribosome and how their association may be tuned by cellular nucleotide status, offering insights into the molecular diversity of ribosome-associated factors and their roles in stress adaptation.
PMID:
42860512
Bibliographic data and abstract were imported from PubMed on 04 Nov 2026.
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