The role of membrane proteins and phospholipids in the interaction of ribosomes with endoplasmic reticulum membranes.
Hydrolysis of the membrane proteins and phospholipid headgroups of rat liver rough endoplasmic reticulum membranes showed that the ribosomal binding sites involve membrane proteins susceptible to low concentrations of trypsin, chymotrypsin, and papain. Three membrane proteins having molecular weights of 120 000, 93 000 and 36 000 are found to be altered by trypsin and chymotrypsin treatment. Also the polar headgroup of phosphatidylinositol appears to play a role in the binding process.
D001665:Binding Sites; D002918:Chymotrypsin; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008099:Liver / Q000378:metabolism / Q000648:ultrastructure; D008566:Membranes / Q000378:metabolism; D008970:Molecular Weight; D010206:Papain; D010740:Phospholipases; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D014357:Trypsin
D010743:Phospholipids; D012269:Ribosomal Proteins; D010740:Phospholipases; D002918:Chymotrypsin; D014357:Trypsin; D010206:Papain