L3(full).txt

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celicachic06
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100137
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L3(full).txt
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2011-09-06 18:30:21
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  1. L3. Activities of the cytoplasm is directed by the_____?
    Nucleus
  2. L3. The part of the cell between the nuclear membrane and the cell membrane is the?
    Cytoplasm
  3. L3.DNA makes RNA..RNA makes?
    Protein
  4. L3. RNA is made in the nucleus and then does what?
    Leaves the nucleus to do its job in cytoplasm
  5. L3.What is transcribed in the nucleolus?
    Ribosomal RNA
  6. L3. Cells that secrete large quantities of protein need more:
    Ribosomes & have larger nucleoli
  7. L3. What forms a ribosome?
    4 different types of ribosomal RNA and the 82 ribosomal proteins that self assemble in the saline environment of the cytoplasm
  8. L3.What is the central dogma of molecular biology?
    DNA makes RNA and RNA makes protein by Sir Francis Crick (w/ mRNA in mind)
  9. L3.Where does the transcription of DNA into complementary mRNA take place?
    �Transcript Domains� in the equatorial plane of the nucleus
  10. L3.What is post-transcriptional processing?
    The removal of the introns and joining of the exons
  11. L3. What small nuclear organelles cut out the introns and join the exons to form usable m-RNA?
    Spliceosomes
  12. L3. A haploid genome contains how many structural genes?
    25,000
  13. L3. All the RNA�s leave the nucleus through what?
    Nuclear pores
  14. L3. Transfer RNA�s binds to a particular amino acid to do what?
    Bring it to the right codon of the m-RNA so it can be incorporated into a protein
  15. L3. What is the carrier protein that RNA is attached to?
    RanGTP
  16. L3. How is the RNA released into the cytoplasm?
    The transport protein lining the nuclear pore binds to RanGTP, uses the energy of the high-energy phosphate bond to transport the RNA-RanGTP complex to the cytoplasmic side of the pore, and then releases the RNA and GDP into the cytoplasm
  17. L3. Ribosomes have to wait for what to specify the amino acid sequence of the protein?
    They must wait for a messenger RNA
  18. L3. Messenger RNA carries what?
    The code for the protein for the ribosome
  19. L3. What is a polyribosome?
    Several ribosomes sharing the same strand of m-RNA
  20. L3. An enzyme specific for an amino acid uses ____ to attached an amino acid to a specific transfer RNA.
    ATP
  21. L3. Transfer RNA-linked amino acid is activated by what?
    By binding GTP
  22. L3. The anticodon on one end of a t-RNA _________bonds to the condon on the mRNA.
    Hydrogen
  23. L3. The large subunit of the ribosome removes what to link each amino acid to the one before it?
    Removes the GTP
  24. L3. Once the AA is linked to the one b4�the mRNA moves how far?
    1 codon or 3 base pairs
  25. L3.When the ribosomes have finished making protens, what drops off?
    m-RNA
  26. L3.M-RNA is tagged by?
    Interfering RNA
  27. L3. The m-RNA is broken down by enzymes in cystoplasmic spots called?
    P-bodies (structure unknown)
  28. L3. Adenosine phosphate, Uridine phosphate, Guanosine phosphate, cytidine phosphate are examples of what?
    Ribonucleotides that return to the nucleus to be reassembled into RNA
  29. L3.What is the constant turnover of m-RNA?
    2 hours
  30. L3. Protein function depends primarily on?
    Shape
  31. L3. Chaperone proteins also known as heat shock proteins do what?
    Catalyze the folding of proteins into the correct shapes
  32. L3. What happens if you have a fever?
    More chaperone proteins are produced to keep the enzyme proteins and structural proteins in correct shapes
  33. L3. What is cytosol?
    Cytoplasm that is not compartmentalized by membranes
  34. L3. Chaperonins are what?
    Cytosolic chaperone proteins that are organized into 11x11 cylinders
  35. L3. What does a chaperonin consist of?
    2 rings, each contains 8 monomers and a protrusion
  36. L3. What�s the job of the protrusion on the chaperonin?
    Recognizes a protein in need of folding and guides it into the cavity formed by the rings
  37. L3. What supplies the energy to fold the proteins into conformity with the cavity?
    Magnesium-activated ATPase
  38. L3. What are prions?
    Misfolded proteins that can cause more proteins of the same type of fold incorrectly ex. Mad cow
  39. L3. Proteins needed in the nucleus are bound to what?
  40. Karyopherin by RanGDP
  41. L3. What is a proteasome?
    • Is when a cytosolic protein is no longer needed and is broken down in this specialized organelle.
    • It�s a small hollow cylinder 15 nm long and 11 nm in diameter. Made up of 4 rings staked
  42. L3. What are on each of 2 end rings of the proteasome?
    It is made up of 7-alpha unit proteins
  43. L3. What are the 2 central rings of the proteasome made of?
    They are made up of 7-beta unit proteins that each have a peptide-bond breaking site
  44. L3. How far apart are the peptide-bond-breaking sites of the beta-unit proteins of the proteasome?
    They are 1.4 nm apart, which is the span of 6 peptide bonds
  45. L3. Making RNA in the nucleus is known as?
    Transcription
  46. L3. Going from RNA to a protein is called what?
    Translation
  47. L3. What breaks down peptides into free amino acids?
    Cytosolic peptidases
  48. L3. What caps the end of a human proteasome?
    Regulatory Protein
  49. L3. The regulatory protein will admit a protein to the proteasome only if its conjugated to a chain of 4 molecules of the small protein, ________?
    Ubiquitin
  50. L3. What is the key step in the regulated destruction of cytosolic proteins?
    Conjugation to ubiquitin
  51. L3. What enzymes prepare ubiquitin for conjugation?
    E1, E2, E3
  52. L3. Which enzyme actually attaches ubiquitin to the protein?
    E3 or ubiquitin ligase
  53. L3. Excess production of an E3 causes what?
    Fatal Deficiency of the protein it tags for destruction
  54. L3. Insufficient production of an E3 can cause what?
    It causes fatal excess of the protein
  55. L3. Theres an absence of E3 for cyclins in what kind of cells?
    Cancer cells
  56. L3. Cancer is caused by the mutation of what protein?
    P53, 55% of cancers have a defective p53

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