Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex | Zendy

Kan Kobayashi | Zendy; Ahmad Jomaa | Zendy; Jae Ho Lee | Zendy; Sowmya Chandrasekar | Zendy; Daniel Boehringer | Zendy; Shuou Shan | Zendy; Nenad Ban | Zendy

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Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex

Author(s) -

Kan Kobayashi,

Ahmad Jomaa,

Jae Ho Lee,

Sowmya Chandrasekar,

Daniel Boehringer,

Shuou Shan,

Nenad Ban

Publication year - 2018

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aar7924

Subject(s) - signal recognition particle , translocon , signal recognition particle receptor , ribosome , endoplasmic reticulum , signal peptide , microbiology and biotechnology , protein targeting , secretory protein , biology , ribosomal protein , chemistry , biochemistry , membrane protein , peptide sequence , secretion , membrane , gene , rna

First steps of translocation elucidated Ribosomes synthesizing membrane or secretory proteins are targeted to the endoplasmic reticulum (ER) in eukaryotic cells by the signal recognition particle (SRP). Upon reaching the ER, the SRP interacts with its receptor to promote transfer of the signal sequence to the protein-conducting channel or translocon. Kobayashiet al. studied the ribosomal complex that forms on the ER, in which the SRP and its receptor interact to transfer the newly synthesized protein to the translocon. The observed organization of the assembly reveals the roles of multiple eukaryotic-specific protein components present in the SRP and its receptor in stabilizing the conformation that facilitates signal sequence handover.Science , this issue p.323

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