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TitleMechanism of cotranslational protein N-myristoylation in human cells.
Journal, issue, pagesMol Cell, Vol. 85, Issue 14, Page 2749-22758.e8, Year 2025
Publish dateJul 17, 2025
AuthorsMartin Gamerdinger / Blanca Echeverria / Alfred M Lentzsch / Nicolas Burg / Ziyi Fan / Mateusz Jaskolowski / Alain Scaiola / Selina Piening / Shu-Ou Shan / Nenad Ban / Elke Deuerling /
PubMed AbstractN-myristoyltransferases (NMTs) cotranslationally transfer the fatty acid myristic acid to the N terminus of newly synthesized proteins, regulating their function and cellular localization. These ...N-myristoyltransferases (NMTs) cotranslationally transfer the fatty acid myristic acid to the N terminus of newly synthesized proteins, regulating their function and cellular localization. These enzymes are important drug targets for the treatment of cancer and viral infections. N-myristoylation of nascent proteins occurs specifically on N-terminal glycine residues after the excision of the initiator methionine by methionine aminopeptidases (METAPs). How NMTs interact with ribosomes and gain timely and specific access to their substrates remains unknown. Here, we show that human NMT1 exchanges with METAP1 at the ribosomal tunnel exit to form an active cotranslational complex together with the nascent polypeptide-associated complex (NAC). NMT1 binding is sequence selective and specifically triggered by methionine excision, which exposes the N-myristoylation motif in the nascent chain. The revealed mode of interaction of NMT1 with NAC and the methionine-cleaved nascent protein elucidates how a specific subset of proteins can be efficiently N-myristoylated in human cells.
External linksMol Cell / PubMed:40639378
MethodsEM (single particle)
Resolution2.8 - 3.43 Å
Structure data

53295

9qqa

EMDB-53295, PDB-9qqa:
Ternary complex of translating ribosome, NAC and NMT1
Method: EM (single particle) / Resolution: 2.8 Å

53296

9qqb

EMDB-53296, PDB-9qqb:
Quaternary complex of a translating ribosome, NAC, NMT1, and NatA
Method: EM (single particle) / Resolution: 3.43 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-UNX:
Unknown entry

ChemComp-SPD:
SPERMIDINE

ChemComp-SPM:
SPERMINE

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

Source
  • oryctolagus cuniculus (rabbit)
  • homo sapiens (human)
KeywordsRIBOSOME / Translation / co-translational protein processing

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