BIOC 212 Lecture Notes - Lecture 18: Prenylation, Hsp70, Gtpase
14 Oct 2015
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Document Summary
Compare and contrast: srp (signal sequence, signal anchor) and hsp70. Atpase vs. gtpase cycle: amino acid modification motifs. Peter walter, reid gilmore, vishwanath lingappa: david andrews, mitochondrial import walter neupert, gottfried schatz, chaperone hypothesis john ellis. Secretory proteins and er: all secretory pathway proteins are synthesized and become folded at the er, misfolded secretory proteins are degraded only at the er. Ubiquitin-proteasome system: only other degradation is at lysosomes, at the end of pathway. Digestion by proteases inside lysosome: er is the protein quality control checkpoint for all organelles in the secretory pathway. Bip and co-chaperones: tm and lumenal erdj proteins activate bip: Assist folding erdj3 is the main substrate-binding (type 1) dnaj. Keep misfolded proteins soluble for degradation: sec63 is a translocon-associated. Protein disulfide isomerase: er lumen is an oxidizing environment, but spontaneous disulfide formation is inefficient and/or incorrect for folding, disulfide formation is catalyzed by thioredoxins:
