2.26.2010

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2.26.2010

  1. 1. 2.26.2010<br /><ul><li>Peroxisomes – Slide 14
  2. 2. Oxidation of long-chain fatty-acids produces H2O2
  3. 3. Decompose/Detoxify H2O2
  4. 4. Catalse generates H20 and O2 from H202
  5. 5. Can utilize organic compounds as a source of H to make water and then leave that dehydrogenated compound as a left-over.
  6. 6. Free ribsomes make proteins for ribosomes that are translated into vesicles and are now peroxisomes
  7. 7. Growth = molecules transported into vesicle
  8. 8. Can undergo fission
  9. 9. Characterized as an isolated organelle
  10. 10. Double material to undergo fission
  11. 11. Can form de novo (from the beginning) from the ER.
  12. 12. Budding of ER and in are the proteins for peroxisomal functions.
  13. 13. Mitochondria
  14. 14. Outer membrane brings components from cytosol through inter membrane space
  15. 15. Review citric acid cycle
  16. 16. Beware of process that produce NADH and FADH2
  17. 17. Pyruvate acetyl coa
  18. 18. Fatty acids to acetyl coa through beta oxidation
  19. 19. Were likely incorporated in eukaryotic cells through phagocytic process
  20. 20. Can replicate itself in cell
  21. 21. Autophagy after 10 days
  22. 22. F1 is ATP generating site
  23. 23. There are 3 beta subunits and 3 alpha subunits in ATP synthase </li></ul>----------------------------------------------------------------------------------------------------------------------------------<br />----Protein Trafficking----<br /><ul><li>Slide 2
  24. 24. All have signal sequence that tell where unit should end up.
  25. 25. Slide 3
  26. 26. SIGNAL SEQUENCES REPRESENT 2 TYPES OF ADDRESSES, SPECIFIC SEQUENCES OF AMINO ACIDS
  27. 27. Signal sequences are strands of amino acids found in the unfolded proteins at Amino or Carboxy terminus. Or in middle of protein
  28. 28. Recognized in an unfolded state
  29. 29. Signal patches are signal sequences that function once when they are brought together and the protein has begun to fold
  30. 30. Near amino terminus,
  31. 31. Hydrophobic amino acids that have some basic positively charged amino acids, followed by hydrophobic amino acids and more basic positively charged amino acids.
  32. 32. Signal sequence for target
  33. 33. Lys-Asp-Glu- provide signal to transport protein into the lumen of the ER
  34. 34. Import into nucleus signal are found in the middleish
  35. 35. Ser-lys-leu is speciic for targeting peroxisomes. (SKL)
  36. 36. KDEL sequence = ER retention signal at carboxy terminus
  37. 37. Slide 4
  38. 38. Mechanisms to bring things back to the ER
  39. 39. Some proteins will be constitutively secreted and others are regulatory proteins.
  40. 40. Slide 5
  41. 41. Anterograde transport from rER to and through golgi occurs by two methods
  42. 42. Vesicular tranport
  43. 43. Only vesicles will bring them back through retro. transport
  44. 44. Cisternal Maturation model
  45. 45. Maturation of tubular clusters that bud off ER.
  46. 46. Maturation of whole cisternae that allows for a transition state
  47. 47. Tubular cluster matures into the cis golgi, medial, trans golgi
  48. 48. Anterograde
  49. 49. Retrograde
  50. 50. Budding of small vesicles off of trans golgi network, through golgi, and into the ER
  51. 51. Slide 6
  52. 52. Pulse-chase experiments
  53. 53. Radio-labeled amino acids to label newly generated proteins w/in the lumen of the ER for about 30 minutes
  54. 54. Pulse:
  55. 55. Specific period when radio-labeled amino acids were ‘bathed’ onto cells
  56. 56. Used pancreatic endocrine cells constantly secrete hormones.
  57. 57. Chase
  58. 58. Unlabeled amino acids added
  59. 59. For a different time period, let the cell rest then fix and analyze where the radio signal is.
  60. 60. Slide 11 – what proteins are involved in each step?
  61. 61. Mutation experiments for KO proteins
  62. 62. Yeast mutagenesis experiments.
  63. 63. Mutant yeast population then try to figure out why they are mutants, characterize the mutation, group them, figure out why they have that mutation
  64. 64. Normal secretion from yeast is a conserved process so you can irradiate yeast
  65. 65. Invertase – developed antibodies to the protein and look where invertase is found, when expressed, and what is its role?
  66. 66. ability to secrete = invertase
  67. 67. Slide 11
  68. 68. We ca change signal sequences for different proteins.
  69. 69. Cytosolic sequence and KDEL sequence maintained in the ER.
  70. 70. Insert ER sequence for cytosolic proteins
  71. 71. Slide 13
  72. 72. SRP recognizes ER signal sequence near N terminus.
  73. 73. Sequence reognition peptide that recognizes ER SS near N terminus
  74. 74. Trans-locon is made of SRP receptor, pore protein, ribosome receptor protein, and a signal peptidase
  75. 75. Pore allows protein to enter ER as being translated
  76. 76. Rib. Receptor binds to large subunit of ribosomal protein to be held during translation
  77. 77. Signal peptidase cuts off signal sequence from protein as being generated.
  78. 78. GTP is hydrolyzied in this process for energy
  79. 79. Translation wont take place until GTP is hydrolyzed
  80. 80. SRP and SRP receptor when hydrolyzed, SRP signal sequence is released and you can begin to translate protein into lumen of the ER
  81. 81. From there, sequences will determine where protein goes, secreted, lysosomes, ER etc.

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