ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane

Nat Struct Mol Biol. 2005 Nov;12(11):1015-6. doi: 10.1038/nsmb998.

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.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cryoelectron Microscopy
  • Endoplasmic Reticulum / metabolism*
  • Gene Expression Regulation / genetics*
  • HSP40 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Membrane Proteins / ultrastructure
  • Mice
  • Models, Molecular*
  • Molecular Chaperones / metabolism
  • Neoplasm Proteins / metabolism*
  • Ribosomes / chemistry*
  • Ribosomes / metabolism
  • Ribosomes / ultrastructure
  • Structure-Activity Relationship

Substances

  • Dnajc1 protein, mouse
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • Neoplasm Proteins
  • molecular chaperone GRP78