Biology 2382B Lecture Notes - Lecture 4: Sucrose, Peptide, Dolichol

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Learning objectives: protein-targeting, er structure and function, contranslational transolocation, protein modifications in er, mitochondrial import of proteins. Structure: uninterrupted membranous tubules and vesicles separated from cytoplasm, rer has ribosomes on the tubules (cisterna, cisterna are stacked, er extend from nuclear membrane. Identify cellular features by microscopy, isolate and homogenize them to free organelles: sucrose density-gradient centrifugation of homogenate allows for isolation of microsomes and ribosomes, sds-page is used to identify newly translated proteins. Er functions: secreted and membrane proteins are sorted through rer, sugars/carbs are added to the polypeptide, disulfide bonds are formed, proteins are folded by chaperones. Major players in rer: amino terminal signal sequence of newly initiated polypeptide (nascent proteins, signal recognition particle (srp, srp receptor embedded in er membrane, translocon: protein channel, cleavage site where signal sequence is cut by a signal peptidase. Protein modifications in er: specific proteolytic cleavage, glycosylation, formation of disulfide bonds, folding of polypeptide chains.

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