Protein Biosynthesis and Maturation in the ER

Abstract

The endoplasmic reticulum takes care of the folding, assembly, and quality control of thousands of proteins destined to the different compartments of the endomembrane system or to be secreted in the apoplast. Here we describe how these early events in the life of all these proteins can be followed biochemically by using velocity or isopycnic ultracentrifugation, metabolic labelling with radioactive amino acids, drug treatments, and immunoselection in various conditions and, in certain cases, predicted in silico by algorithms.

Keywords: Chaperones; Endoplasmic reticulum; Immunoglobulin binding protein (BiP); Immunoselection; Protein folding; Protein oligomerization; Protein synthesis; Protein-protein interactions; Pulse-chase; Ultracentrifugation.