核糖体
蛋氨酸
核糖体生物发生
生物发生
内质网
核糖体蛋白
细胞生物学
生物化学
蛋白质生物合成
生物
多形体
化学
氨基酸
核糖核酸
基因
作者
Martin Gamerdinger,Min Jia,Renate Schloemer,Laurenz Rabl,Mateusz Jaskółowski,Katrin M. Khakzar,Zeynel Ulusoy,Annalena Wallisch,Ahmad Jomaa,Gundula Hunaeus,Alain Scaiola,Kay Diederichs,Nenad Ban,Elke Deuerling
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2023-06-23
卷期号:380 (6651): 1238-1243
被引量:3
标识
DOI:10.1126/science.adg3297
摘要
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.
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