BIOL 200 Chapter Notes - Chapter 4: Secretion, Ubiquitin, Peptide
Document Summary
Rer (with ribosomes docked onto them) and ser are always connected: describe how proteins are targeted and imported into the endoplasmic reticulum and compare these mechanisms to protein targeting and import into the nucleus. Must be present for a protein to leave the cytosol compartment. Can leave nucleus with nes: predict the signal sequences required to insert a protein into the er membrane in any orientation, and predict protein topology from a corresponding domain map. Domain mapping: used to show predicted regions with specific function in primary sequence of a protein. N-terminal signal sequence: n terminal in er start transfer sequence: n-terminal in cytosol: discuss the role of chaperones in protein folding and role of proteasomes in quality control of misfolded proteins in the secretory pathway. Chaperone proteins: form complex with polypeptides, binding to specific region that facilitate folding or provide protected space away from rest of cytosol so protein can fold in isolation (prevent misfolds)
