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Structure paper

TitleNAC guides a ribosomal multienzyme complex for nascent protein processing.
Journal, issue, pagesNature, Vol. 633, Issue 8030, Page 718-724, Year 2024
Publish dateAug 21, 2024
AuthorsAlfred M Lentzsch / Denis Yudin / Martin Gamerdinger / Sowmya Chandrasekar / Laurenz Rabl / Alain Scaiola / Elke Deuerling / Nenad Ban / Shu-Ou Shan /
PubMed AbstractApproximately 40% of the mammalian proteome undergoes N-terminal methionine excision and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferase A (NatA), ...Approximately 40% of the mammalian proteome undergoes N-terminal methionine excision and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferase A (NatA), respectively. Both modifications are strictly cotranslational and essential in higher eukaryotic organisms. The interaction, activity and regulation of these enzymes on translating ribosomes are poorly understood. Here we perform biochemical, structural and in vivo studies to demonstrate that the nascent polypeptide-associated complex (NAC) orchestrates the action of these enzymes. NAC assembles a multienzyme complex with MetAP1 and NatA early during translation and pre-positions the active sites of both enzymes for timely sequential processing of the nascent protein. NAC further releases the inhibitory interactions from the NatA regulatory protein huntingtin yeast two-hybrid protein K (HYPK) to activate NatA on the ribosome, enforcing cotranslational N-terminal acetylation. Our results provide a mechanistic model for the cotranslational processing of proteins in eukaryotic cells.
External linksNature / PubMed:39169182
MethodsEM (single particle)
Resolution3.01 - 6.67 Å
Structure data

50124

9f1b

EMDB-50124, PDB-9f1b:
Mammalian ternary complex of a translating 80S ribosome, NAC and NatA/E
Method: EM (single particle) / Resolution: 3.01 Å

50125

9f1c

EMDB-50125, PDB-9f1c:
Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E
Method: EM (single particle) / Resolution: 3.78 Å

50126

9f1d

EMDB-50126, PDB-9f1d:
Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E-HYPK
Method: EM (single particle) / Resolution: 3.26 Å

EMDB-50127: Mammalian ternary complex of a translating 80S ribosome, NAC and NatA/E - local refinement
Method: EM (single particle) / Resolution: 6.45 Å

EMDB-50128: Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E - local refinement
Method: EM (single particle) / Resolution: 6.67 Å

EMDB-50129: Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E-HYPK - local refinement
Method: EM (single particle) / Resolution: 5.75 Å

EMDB-50130: Mammalian ternary complex of an 80S ribosome, NAC and NatA/E
Method: EM (single particle) / Resolution: 3.21 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-UNX:
Unknown entry

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

ChemComp-SPD:
SPERMIDINE

ChemComp-SPM:
SPERMINE

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • oryctolagus cuniculus (rabbit)
  • homo sapiens (human)
  • schistosoma japonicum (invertebrata)
KeywordsTRANSLATION / ribosome / N-terminal acetyltransferase / NatA / NatE / NAC / MetAP1 / HYPK

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