1. DnaK (E. coli Hsp70) consists of two domains: 44-kD N-terminal ATP-binding domain 18-kD central domain that binds peptides with exposed hydrophobic regions
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2. DnaK mechanism of action
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3. DnaK mechanism of action
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4. Slide 16
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5. Hsp60 Chaperonin
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6. E. coli Hsp60 Chaperonin GroES-GroEL
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7. Hsp60 Chaperonin
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8. E. coli Hsp60 Chaperonin GroES-GroEL
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9. Figure 31.3 (a) Structure and overall dimensions of GroES-GroEL. (b) Section through the center of the complex to reveal the central cavity
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10. GroES-GroEL mechanism of action
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11. Figure 31.3 (a) Structure and overall dimensions of GroES-GroEL. (b) Section through the center of the complex to reveal the central cavity
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12. E. coli Hsp60 Chaperonin GroES-GroEL
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13. Hsp60 Chaperonin
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14. E. coli Hsp60 Chaperonin GroES-GroEL
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15. Figure 31.3 (a) Structure and overall dimensions of GroES-GroEL. (b) Section through the center of the complex to reveal the central cavity
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16. GroES-GroEL mechanism of action
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17. Slide 21
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18. GroES-GroEL mechanism of action
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19. Slide 21
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20. The eukaryotic group II chaperonin
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21. Slide 21
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22. GroES-GroEL mechanism of action
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23. Slide 21
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24. GroES-GroEL mechanism of action
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25. Slide 21
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26. GroES-GroEL mechanism of action
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27. Slide 21
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28. The eukaryotic group II chaperonin
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29. Group II chaperonin
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30. Prefoldin structure
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31. Figure 31.3 (d)
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32. The eukaryotic Hsp90 Chaperones Act on Proteins of Signal Transduction Pathways
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33. 31.2 How Are Proteins Processed Following Translation?
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34. Proteolytic cleavage is the most common form of post-translational modification
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35. Slide 29
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36. 31.3 How Do Proteins Find Their Proper Place in the Cell?
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37. Proteins are delivered to their proper cell compartment by translocation
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38. Proteins to be translocated are made as preproteins containing signal sequencesPreprotein are maintained in a loosely folded, translocation-competent conformation through interaction with chaperonesEukaryotic chaperones within membrane compartment are usu
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39. The four compartments in Gram (-) bacteria
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40. Prokaryotic proteins destined for translocation are synthesized as preproteins
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41. Eukaryotic Proteins Are Delivered to Locations by Protein Sorting and Translocation
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42. Recognition by the ER:
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43. Synthesis of Secretory Proteins and Many Membrane Proteins is Coupled to Translocation
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44. Interaction between the RNC-SRP and the SR Delivers the RNC to the membrane
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45. Ribosome and Translocon Form a Common Conduit for Nascent Protein Transfer
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46. After entering ER, the signal peptide is clipped off by membrane-bound signal peptidase (leader peptidase)Secretory proteins enter ER completely Membrane proteins have stop-transfer sequences that arrest the passage across ER Stop-transfer: 20-residue st
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47. Slide 41
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48. Translocation of membrane protein
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49. Figure 31.5 Synthesis of a eukaryotic secretory protein and its translocation into the ER
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50. Other post-translational modifications occurs, glycosylationMammalian translocon: Sec61 complex (a, b, g) + TRAMSec61 complex forms the channel; dynamic pore size, 0.6 – 6 nmTRAM inserts the nascent integrate membrane proteins into membrane.
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51. Retrograde Translocation Prevents Secretion of Damaged Proteins and Recycles Old ER Proteins
56. Translocation of Mitochondrial Preproteins Involves Distinct Translocons
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57. Figure 31.7 All mitochondrial proteins must interact with the outer mitochondrial membrane (TOM). They can be passed to the SAM complex or enter the intermembrane space.
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58. 31.4 How Does Protein Degradation Regulate Cellular Levels of Specific Proteins?
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59. Eukaryotic proteins are targeted for proteasome destruction by ubiquitination
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60. The three proteins involved in ubiquitination E1, E2, and E3
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61. Slide 54
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62. Enzymatic Reactions in the Ligation of Ubiquitin to Proteins
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63. Slide 56
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64. E3 recognizes and selects protein for degradation
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65. E3 recognizing N-terminal amino acid
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66. Figure 31.9 Arginyl-tRNAArg:protein transferase transfers Arg to the free α-NH2 of proteins with Asp or Glu N-termini. Arg-tRNAArg:protein transferase serves as part of the protein degradation recognition system.
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67. E3 recognizing N-terminal amino acid
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68. Figure 31.9 Arginyl-tRNAArg:protein transferase transfers Arg to the free α-NH2 of proteins with Asp or Glu N-termini. Arg-tRNAArg:protein transferase serves as part of the protein degradation recognition system.
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69. Proteins Targeted for Destruction Are Degraded by Proteasomes
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70. Thermoplasma acidophilum 20S proteasome
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71. Eukaryotic Cells Contain Two Forms of Proteasomes
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72. The 26S Proteasome is Composed of a 20S Proteasome Plus 19S Regulator Caps
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73. 19S regulator: lid + base
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74. The Ubiquitin-ProteasomeDegradation Pathway
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75. Small Ubiquitin-Like Protein Modifiers Are Post-Translational Regulators
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76. The Mechanism of Reversible Sumoylation
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77. The Molecular Consequences of Sumoylation
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78. Ubc9 is the only known SUMO E2 enzyme, which recognize yKXD/E The recognition site should be in a relative unstructured part of a target protein or in an extended loopSumoylation is involved in transcriptional regulation, chromosome organization, nuclear
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79. The Structure of an E2 Enzyme:Target Protein Complex
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80. HtrA Proteases Also Function in Protein Quality Control
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81. Prokaryotic HtrA proteases act as chaperones at low temperatures (20°C), but as temperature rises they become a protease to remove misfolded or unfolded proteins DegP (from E. coli) is the best characterized HtrA proteaseDegP is localized in periplasm to