考研资料：北京大学细胞生物学第6章基质与内膜(下).pptVIP

B. Signal Hypothesis --G.Blobel D.Sabatini,1971. A model for the Signal Mechanism of Cotranslational Import;Milstein et al: Studying the synthesis of light chain of IgG (in cell-free systems, 20 Aa longer at N-terminal end than the authentic light chain ); ;Signal-recognition particle, SRP: Six different polypeptides complexed with a 300-nucleotide (7S)molecule of RNA. ER signal sequence: Typically 15-30 amino acids: Consist of three domains: a positively charged N-terminal region, a central hydrophobic region, and a polar region adjoining the site where cleavage from the mature protein will take place. A signal sequence on nascent seretory proteins targets them to the ER and is then cleaved off SRP receptor (GTP binding protein);The sorting signal of VSV glycoproteins : Asp-X-Gln或DXE;Start-transfer Sequence Stop-transfer Sequence;Figure 6-24. Synthesis and insertion into the ER membrane of the GLUT1 glucose transporter and other proteins with multiple transmembrane a-helical segments. The N-terminal a helix functions as an internal, uncleaved signal-anchor sequence (red), directing binding of the nascent polypeptide chain to the rER membrane and initiating cotranslational insertion. Both SRP and the SRP receptor are involved in this step. Following synthesis of helix 2, which functions as a stop-transfer membrane-anchor sequence, extrusion of the chain through the translocon into the ER lumen ceases. The first two a helices then move out of the translocon into the ER bilayer, anchoring the nascent chain as an a-helical hairpin. The C-terminus of the nascent chain continues to grow in the cytosol. Subsequent a-helical hairpins could insert similarly, although SRP and the SRP receptor are required only for insertion of the first signalanchor sequence. Although only six transmembrane a helices are depicted here, GLUT1 and proteins of similar structure have twelve or more. [H. P. Wessels et al., Cell 55:61.] ;The Orientation o