ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane.
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.
Blau
Michael
M
Institut für Biochemie der Charité, University Medical School Berlin, Monbijoustr. 2, 10117 Berlin, Germany.
Mullapudi
Srinivas
S
Becker
Thomas
T
Dudek
Johanna
J
Zimmermann
Richard
R
Penczek
Pawel A
PA
Beckmann
Roland
R
D000818:Animals; D020285:Cryoelectron Microscopy; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D000091342:Endoplasmic Reticulum Chaperone BiP; D005786:Gene Expression Regulation / Q000235:genetics*; D050956:HSP40 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D051379:Mice; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D013329:Structure-Activity Relationship
C092319:Dnajc1 protein, mouse; D000091342:Endoplasmic Reticulum Chaperone BiP; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins