BIOL 2021 Lecture Notes - Lecture 7: Mitochondrial Matrix, Signal Peptidase, Intermembrane Space
9 Feb 2018
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Document Summary
Protein goes through two translocators, one in each of the membranes. Once inside, a signal peptidase, cleaves the peptide and the chaperone protein leaves and the protein folds into a three dimensional structure. Protein import by mitochondria: 1) precursor protein synthesized in cytosol = post-translational import. Binds to cytosolic chaperone protein (hsp70) prevent protein from folding. It"s part of the energy source that makes sure the protein stays in there and doesn"t go back. It binds to the protein and helps pool it into the matrix, preventing it from backsliding through tim: 7) signal sequence cleaved off by peptidase. The signal sequence, sequences the protein to the mitochondria. Some of these interacting proteins are general chaperone proteins of the hsp70 family. All the interacting proteins help to prevent the precursor proteins from aggregating or folding up spontaneously before they engage with the tom complex in the outer mitochondrial membrane.
