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Title | NAC controls cotranslational N-terminal methionine excision in eukaryotes. |
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Journal, issue, pages | Science, Vol. 380, Issue 6651, Page 1238-1243, Year 2023 |
Publish date | Jun 23, 2023 |
Authors | Martin Gamerdinger / Min Jia / Renate Schloemer / Laurenz Rabl / Mateusz Jaskolowski / Katrin M Khakzar / Zeynel Ulusoy / Annalena Wallisch / Ahmad Jomaa / Gundula Hunaeus / Alain Scaiola / Kay Diederichs / Nenad Ban / Elke Deuerling / |
PubMed Abstract | N-terminal methionine excision from newly synthesized proteins, catalyzed cotranslationally by methionine aminopeptidases (METAPs), is an essential and universally conserved process that plays a key ...N-terminal methionine excision from newly synthesized proteins, catalyzed cotranslationally by methionine aminopeptidases (METAPs), is an essential and universally conserved process that plays a key role in cell homeostasis and protein biogenesis. However, how METAPs interact with ribosomes and how their cleavage specificity is ensured is unknown. We discovered that in eukaryotes the nascent polypeptide-associated complex (NAC) controls ribosome binding of METAP1. NAC recruits METAP1 using a long, flexible tail and provides a platform for the formation of an active methionine excision complex at the ribosomal tunnel exit. This mode of interaction ensures the efficient excision of methionine from cytosolic proteins, whereas proteins targeted to the endoplasmic reticulum are spared. Our results suggest a broader mechanism for how access of protein biogenesis factors to translating ribosomes is controlled. |
External links | Science / PubMed:37347872 |
Methods | EM (single particle) |
Resolution | 2.9 Å |
Structure data | EMDB-17367, PDB-8p2k: |
Chemicals | ChemComp-N: ChemComp-SPD: ChemComp-SPM: ChemComp-MG: ChemComp-UNX: ChemComp-GTP: ChemComp-AAC: ChemComp-ZN: ChemComp-HOH: |
Source |
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Keywords | TRANSLATION / ribosome / methionine aminopeptidase 1 / methionine excision / protein biogenesis / nascent chain |