Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle
| Autor: | Kan Kobayashi, Zikun Zhu, Shu-ou Shan, Sowmya Chandrasekar, Simon Eitzinger, Nenad Ban, Ahmad Jomaa |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Signal peptide
Models Molecular Receptors Peptide QH301-705.5 co-translational protein targeting cryoelectron microscopy Receptors Cytoplasmic and Nuclear GTPase medicine.disease_cause Ribosome Models Biological environment and public health General Biochemistry Genetics and Molecular Biology Article GTP Phosphohydrolases Protein Domains Protein targeting medicine Animals Humans signal recognition particle signal peptide Biology (General) Ribosome-nascent chain complex Mammals Signal recognition particle GTPases Bacteria Chemistry Endoplasmic reticulum RNA transmembrane domain ribosome nascent chain complex endoplasmic reticulum Cell biology Protein Transport |
| Zdroj: | Cell reports Cell Reports, Vol 36, Iss 2, Pp 109350-(2021) Cell Reports, 36 (2) |
| ISSN: | 2666-3864 2211-1247 |
| DOI: | 10.3929/ethz-b-000495624 |
| Popis: | Co-translational protein targeting to membranes by the signal recognition particle (SRP) is a universally conserved pathway from bacteria to humans. In mammals, SRP and its receptor (SR) have many additional RNA features and protein components compared to the bacterial system, which were recently shown to play regulatory roles. Due to its complexity, the mammalian SRP targeting process is mechanistically not well understood. In particular, it is not clear how SRP recognizes translating ribosomes with exposed signal sequences and how the GTPase activity of SRP and SR is regulated. Here, we present electron cryo-microscopy structures of SRP and SRP·SR in complex with the translating ribosome. The structures reveal the specific molecular interactions between SRP and the emerging signal sequence and the elements that regulate GTPase activity of SRP·SR. Our results suggest the molecular mechanism of how eukaryote-specific elements regulate the early and late stages of SRP-dependent protein targeting. Cell Reports, 36 (2) ISSN:2666-3864 ISSN:2211-1247 |
| Databáze: | OpenAIRE |
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