508lecture35

508lecture35 - Lecture 35 Review Sunday 1-4pm room 2-147 TD review starts at 2:30 Continued from lecture 34(see cartoon diagram Degradation through

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Lecture 35 5/12/04 Review Sunday 1-4pm room 2-147 TD review starts at 2:30 Continued from lecture 34 (see cartoon diagram) Degradation through poklyubiquitination- (eucaryotes) Specificity comes from E3 (remember ~100 E3’s inside the cell) You could imagine one type of E3 would interact with positively charged N-terminal amino acid, and another would recognize hydrophobic N-term. Several ubiquitins are added on to a lysine on the protein by E3 and E2 Ubiquitination may have many roles inside the cell- we are only discussing its role in protein degradation in yeast. Roles of E1,E2,E3 in ubiquitination (See handout 4d for cartoons of all of this) 1) ATP activated Ub through adenylation 2) E1 binds covalently to C-term of Ub through a thioester Need fewer E1-> higher turnover rate than E2, E3 3) Ub transferr to E2, again as a thioester 4) Substrate needs N-end amino acid + lysine-> E3 interacts with substrate and E2 to catalyze attachment oof Ub to lysine through isopeptide linkage 5) Next Ub is added onto the lysine 48 of the previous Ub (E2, E3 repeat same
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This note was uploaded on 11/11/2011 for the course BIO 7.012 taught by Professor Lander during the Fall '10 term at MIT.

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508lecture35 - Lecture 35 Review Sunday 1-4pm room 2-147 TD review starts at 2:30 Continued from lecture 34(see cartoon diagram Degradation through

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