Abstract
Ribosomes translating secretory and membrane proteins are targeted to the endoplasmic reticulum membrane and attach to the protein-conducting channel and ribosome-associated membrane proteins (RAMPs). Recently, a new RAMP, ERj1p, has been identified that recruits BiP to ribosomes and regulates translational activity. Here we present the cryo-EM structure of a ribosome–ERj1p complex, revealing how ERj1p coordinates the ribosome at the membrane and how allosteric effects may mediate ERj1p's regulatory activity.
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Acknowledgements
This work was supported by grants from the VolkswagenStiftung (R.B.), Deutsche Forschungsgemeinschaft (R.Z., J.D. and grant Sfb449 to M.B. and R.B.) and from the US National Institutes of Health (R01 NS 43258 and R01 GM 60635 to P.A.P.). The technical assistance of A. Müller is gratefully acknowledged. The cryo-EM data were collected, in part, on the JEOL 3000SFF electron microscope at the National Center for Macromolecular Imaging (Houston, USA), which is supported by the US National Institutes of Health though the National Center for Research Resources's P41 program (grant RR02250). We thank A. Paredes for his microscopy work.
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Blau, M., Mullapudi, S., Becker, T. et al. ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane. Nat Struct Mol Biol 12, 1015–1016 (2005). https://doi.org/10.1038/nsmb998
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DOI: https://doi.org/10.1038/nsmb998
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