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TitleThe ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis.
Journal, issue, pagesMol Cell, Year 2026
Publish dateJan 19, 2026
AuthorsAlžběta Roeselová / Santosh Shivakumaraswamy / Gabija Jurkeviciute / Jessica Zhiyun He / Josef Auburger / Jaro L Schmitt / Günter Kramer / Bernd Bukau / Radoslav I Enchev / David Balchin /
PubMed AbstractNatural proteins often form intricate multidomain, oligomeric architectures. This presents a prima facie challenge to cellular homeostasis, as topologically complex proteins seldom refold efficiently ...Natural proteins often form intricate multidomain, oligomeric architectures. This presents a prima facie challenge to cellular homeostasis, as topologically complex proteins seldom refold efficiently in vitro. Here, we show that the efficient folding and assembly of the five-domain homotetramer β-galactosidase is obligatorily coupled to its synthesis on the ribosome, and we define the underlying mechanisms. During refolding from a denaturant, maturation of the catalytic domain is frustrated. Assembly outpaces monomer folding, and non-native oligomers accumulate. Efficient de novo folding is characterized by segmental domain folding, shaped by the binding of a nascent amphipathic helix to a cryptic pocket on uL23 on the ribosome surface. Homomer assembly also initiates cotranslationally via recruitment of a full-length subunit to the nascent polypeptide, and the failure to do so results in misassembly. Our results reveal how the ribosome can dictate the timing of folding and assembly to enable efficient biogenesis of a topologically complex protein.
External linksMol Cell / PubMed:41558483
MethodsEM (single particle)
Resolution2.86 Å
Structure data

53553

9r3a

EMDB-53553, PDB-9r3a:
Structure of Stalled Beta-Galactosidase 70S Ribosome Nascent Chain
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-PRO:
PROLINE

Source
  • escherichia coli bl21(de3) (bacteria)
  • escherichia coli (E. coli)
KeywordsRIBOSOME / translation / co-translational folding / nascent chain / protein folding

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