Translation LO Flashcards Preview

M2M Biochemistry and molecular biology > Translation LO > Flashcards

Flashcards in Translation LO Deck (72):
1

what is the central dogma?

DNA to RNA to Protein

2

how many high-energy bonds are formed for each peptide bond?

4

3

True of False
the basic process of translation is highly conserved between all forms of life

True

4

what is the function of messenger RNA (mRNA)?

carries codons that code for the amino acid sequence of a protein

5

how many possible codons are there?

4^3= 64 possible codons

6

What is the start codon?

AUG

7

what are the "non-sense" or stop codons on RNA?

UGA
UAA
UAG

8

what is the function of transfer RNA (tRNA)?

"read" the message and deliver the right amino acid to the ribosome

9

what dictates the function of tRNA?

the three-dimensional folded structure

10

why can some tRNA's recognize more than one codon?

wobble-pairing at the third location on the codon

11

what is the function of aminoacyl tRNA synthetases?

protein enzymes that put the right amino acid on the right tRNA

12

what is the function of the ribosome?

catalytic center for translation

13

what synthetase puts a valine on a val-tRNA?

valyl-tRNA synthetase
(aminoacid-tRNA synthetase)

14

what are the 2 subunits in prokaryotic ribosomes?

30S and 50S

15

what are the 2 subunits in eukaryotic ribosomes?

30S and 60S

16

which subunit contains the catalytic center?

the large subunit

17

what is another name for the catalytic center of a ribosome?

peptidyl transferase center (PTR)

18

what type of enzyme is a ribosome and why?

ribozyme because it uses RNA to perform catalysis

19

what is the function of initiating factors in translation?

bring ribosome to the message and assist in getting the machinery assembled

20

what is the function of elongation factors and their partners?

deliver tRNAs and move ribosome down the message

21

what is the function of termination/recycling factors?

end the process at stop codon, disassociate subunits so they can be used again

22

where is the amino acid attached on tRNA?

the acceptor stem

23

which portion of the tRNA reads the mRNA?

anticodon loop

24

what is the start codon and which amino acid does it code for?

AUG
methionine

25

what is the final assembled ribosome called in prokaryotes?

70S

26

what is the final assembled ribosome called in eukaryotes?

80S

27

how many tRNA binding sites does a ribosome have?

3

28

what are the 3 binding sites on a ribosome?

A- aminoacyl site
P - peptidyl site
E - exit site

29

what are the 4 phases of translation?

1. initiation
2. elongation
3. termination
4. ribosome recycling

30

which step in translation differs the most between eurkaryotes and prokaryotes?

initiation

31

what is the point of the initiation step?

assemble ribosome at start codon (AUG) with initiator methionine tRNA in P-site and next aa-tRNA in the A-site

32

what initiation factor proteins are used in prokaryotes to bind the 30S subunit?

IF1 and IF3

33

what is the function of IF2 in prokaryotes?

delivers special "initiator" formylmethionine tRNA to P-site to pair with AUG codon

34

what does GTP hydrolysis of IF2 lead to?

release of all initiation factors and binding of 50S subunit forming 70S ribosome

35

why does the ribosome in prokaryotes bind directly to the AUG codon?

Shine-Dalgarno sequence about 8 bp upstream from AUG codon

36

what initiation factor in eukaryotes binds the 7-methyl guanosine cap to the 5' end of RNA?

4E

37

what does polycistronic mean?

mRNA can have many genes expressed on just one strand such as in prokaryotes (have many shine-dalgarno sites) (lac operon)

38

how is eukaryotic initiation different than prokaryotic initiation?

eukaryotic more complex, ribosome scans downstream to find AUG codon after small subunit binds and then large subunit can bind, prokaryotes bind directly to AUG codon

39

which step of translation is considered to have the most control and regulation?

initiation

40

what is elongation?

moving along the mRNA and making the encoded protein

41

where does the energy for peptide bond formation come from?

ATP used in tRNA charging

42

what moves the mRNA and tRNAs exactly one codon in the 3' direction?

EF2 and GTP hydrolysis

43

what are the 4 high energy bonds expended to form a peptide bond?

1. charge tRNA (2 ATP to AMP)
2. deliver aa-tRNA to A site (1 GTP to GDP)
3. translocation (1 GTP to GDP)

44

which factors bind to the stop codon and terminate the polypeptide synthesis?

release factors

45

what is a missense mutation?

mutation resulting in amino acid change

46

what is a silent mutation?

codon is changed but same amino acid is encoded (the mutation is in the wobble position)

47

what is a frame-shift mutation?

an addition or deletion of a nucleotide causes a shift in the reading frame

48

what is a non-sense mutation?

mutation resulting in a premature stop codon

49

what is a sense mutation?

mutation resulting in a removed stopped codon

50

what mutation is Hemoglobin Wayne a result of?

3' terminal frameshift mutation

51

what mutation is Hemoglobin Constant Spring a result of?

Sense mutation (UAA stop to CAA Gln)+

52

what presentation do both Hemoglobin Wayne and Hemoglobin Constant Spring have?

chronic anemia

53

why can production of protein be slowed if a mutation gives rise to a "rare" codon?

because there are a limited number of tRNA for each amino acid

54

what determines the strength of expression of different AUG's in eukaryotes?

Kozak Context

55

what is RNA editing and why is it significant?

transcribed RNA modified so that coding is affected. important because some proteins are tissue specific, can have 2 types of protein from 1 gene that is tissue specific (apoB)

56

transferrin

binds iron

57

transferrin receptor (TFR)

transports Fe into the cell

58

ferritin

sequesters excess FE

59

iron repsponse element (IRE)

RNA stem-loop structure found in mRNAs that can bind to IRPs

60

Irons Response Binding proteins (IRE-BPs) 1 and 2

bind FE and regulate expression of ferritin and TFR

61

under high Fe conditions, what is the relationship between IRE-BPs, Fe, and IRE RNA

IRE-BPs bound to Fe
IRE-BPs cannot bind to IRE RNA

62

under low Fe conditions what is the relationship between IRE-BPs, Fe, and IRE RNA?

IRE-BPs not bound to Fe
IRE-BPs can bind to IRE RNA

63

What happens to the level of transferrin receptor protein in low iron conditions?

protein level increases

64

what happens to the level of transferrin receptor protein in high iron conditions?

protein level decreases

65

what is the mechanism of transferrin receptor protein regulation?

in low iron situations, IRE-binding protein binds to IRE of mRNA protecting the mRNA strand from being degraded and thus synthesis continues (opposite in high iron situations)

66

what happens to ferritin levels in low iron concentrations?

decrease

67

what happens to ferritin levels in high iron concentrations?

increases

68

what is mechanism of ferritin regulation?

in low iron situations, IRE-BP binds to IRE thus inhibiting ferritin synthesis because IRE prior to start codon (opposite in high concentration)

69

what is cap-independent translation?

mRNA does not require cap to initiate synthesis, instead has internal ribosomal entry site (IRES) which can recruit the subunit

70

why is cap-independent translation important for viruses?

because virus can shut down cap-dependent translation by cleaving eIF4G in the eukaryotic cell but continue replicating its own RNA

71

how does mTOR regulate eIF4E?

mTOR can induce phosphorylation on the eIF4E-binding protein thus dissociating the binding protein from the initiating factor thus allowing translation to occur

72

what is the process of interferon signaling?

cell infected by virus, infected cell creates interferons which signals other cells to create anti-viral measures (eIF2 kinase), virus cannot proliferate in cells notified by initial infected translation machinery shut off