第七章 细胞质基质与细胞内膜系统PPT.ppt

* * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * Synthesis and Insertion into the ER Membrane of the GLUT1 Glucose Transporter and Other Proteins with Multiple Transmembrane α-helical Segments. The N-terminal α helix functions as an internal, uncleaved signal-anchor sequence (red), directing binding of the nascent polypeptide chain to the rough ER 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 α helices then move out of the translocon into the ER bilayer, anchoring the nascent chain as an α helical hairpin. The C-terminus of the nascent chain continues to grow in the cytosol. Subsequent α helical hairpins could insert similarly, althrough SRP and the SRP receptor are required only for insertion of the first signal-anchore sequence. Althrough only six transmembrane α helices are dipicted here, GLUT1 and proteins of similar structure have twelve or more. 导肽与后转移 (Leader peptide and Post translocation) ?基本的特征： 　　蛋白质在细胞质基质中合成以后再转移到细胞器中，称为后转移(post translocation)。 　　蛋白质跨膜转移过程需要ATP使多肽去折叠，还需要一些蛋白质的帮助 (如热休克蛋白Hsp70) 使其能够正确地折叠成有功能的蛋白。 后转移 A Model for the Posttranslational Import of Polypeptides into the Mitochondrion. Like cotranslational import into the ER, posttranslational import into a mitochondrion involves a signal sequence (called a transit sequence in this case), a membrane receptor, pore-forming membrane proteins, and a peptidase. However, in the mitochondrion, the membrane receptor recognizes the signal sequence directly, without the intervention of a cytosolic SRP. Furthermore, chaperone proteins play several crucial roles in the mitochondrial process. They keep the polypeptide partially unfolded after synthesis in the cytosol so that binding of the transi