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Molecular Biology and Genetics > Genes and proteins: Translation of RNA into proteins > Flashcards

Genes and proteins: Translation of RNA into proteins Flashcards

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1
Q

What does the link between DNA coding and resulting peptide involve?

A

DNA transcription by RNA Polymerase.

mRNA translation by ribosomes.

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2
Q

Of what do proteins consist?

A

Amino acid chains.

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3
Q

How are the amino acid chains structured in proteins?

A

Linked together.

Specific order.

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4
Q

How is the specific order of amino acid chains in proteins called?

A

The primary structure.

From N-terminus to C-terminus.

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5
Q

What can the peptide chain adopt over time?

A

Different structures fold around itself.

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6
Q

What happens when peptide chains adopt different structures?

A

They interact with one another –> form the final protein.

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7
Q

How many common amino acids are found in proteins?

A

20.

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8
Q

What are the characteristics of the 20 common amino acids in proteins?

A 
Different:
Sizes.
Polarity.
Hydrophobicity.
Charge.
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9
Q

How are the amino acids referred?

A

Single/3 -letter codes.

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10
Q

How can amino acids be categorised?

A

By:
Polarity.
Charge.
Size.

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11
Q

In how many levels polypeptide chains fold and interact with other chains?

A

4.

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12
Q

Why do polypeptide chains fold and interact with each other?

A

To produce the final 3-dimensional shape of the mature protein.

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13
Q

How are the amino acids arranged in a peptide chain?

A

Linear.

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14
Q

What does the linear arrangement of amino acids in a peptide chain produce?

A

Structural limitations.

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15
Q

What are the characteristics of the secondary structure of peptide chains?

A 
Limited flexibility.
Forced shape = 
α helices
β sheets
random coils
loops.
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16
Q

Which factors stabilise the structure of peptides?

A

Hydrogen bonds.
Hydrophobic interactions.
Ionic bonds.
Disulphide linkages.

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17
Q

How do bonds and linkages stabilise the structure of the peptide?

A

By connecting different parts of it.

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18
Q

Where are the R groups of amino acids presented?

A

On the outside surface of the protein.

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19
Q

What is a common active site in enzymes?

A

The ‘catalytic triad’.

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20
Q

How is the ‘catalytic triad’ formed in an enzyme?

A

3-dimensional positions:

  1. R groups.
  2. Acid nucleophile.
  3. Base nucleophile.
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21
Q

What happens in translation process of RNA?

A

Genetic information encoded by DNA –> transcribed into mRNA –> converted into –> amino acid sequences –> polypeptides.

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22
Q

What does the RNAP do in RNA translation?

A

Uses template DNA double-stranded helix –> produces mRNA.

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23
Q

What is the produced mRNA based on the coding strand?

A

Equivalent.

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24
Q

What does the amino acid sequence do in RNA translation process?

A

It follows the coding strand.

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25
Q

What does the genetic use to encode the amino acids in a peptide chain?

A

Triplets of DNA bases.

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26
Q

How is the genetic code characterised?

A

Almost universal.

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27
Q

How many combinations of A, C, G, and T exist?

A

> 20.

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28
Q

What do some amino acids have?

A

> 1 triplet.

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29
Q

How are some triplets used?

A

As stop signals.

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30
Q

Where are amino acids matched to base triplets?

A

In the ribosome.

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31
Q

By which factor are amino acids matched to base triplets?

A

By tRNAs.

32
Q

What does the universal code link?

A

RNA triplets - amino acids.

DNA triplets - amino acids.

33
Q

How many over-lapping reading frames does a section of double-stranded DNA have that encode a protein?

A

6.

34
Q

How many reading frames are used at a time?

A
  1. Start-codon.
    Stop codon.
35
Q

What is something uncommon?

A

Over-lapping genes.

36
Q

What is the most usual start codon?

A

AUG.

37
Q

What are the most usual in-frame stop codons?

A

UAA.
UAG.
UGA.

38
Q

Where does the 5’ start of the DNA coding map?

A

To the 5’ start of the mRNA transcript + first N-terminal amino acid of protein.

39
Q

Where does the 3’ end of the DNA coding map?

A

To the 3’ end of mRNA transcript + last C-terminal amino acid.

40
Q

Where does the 3’ end of DNA coding not map?

A

To the poly-A tail.

41
Q

By what is the stop codon not represented?

A

An amino acid.

42
Q

What are the tRNAs?

A

Short RNA molecules.

43
Q

What is the structure of tRNAs?

A

‘t’.
‘L’.
Neck linked to specific amino acid.
Foot matches mRNA triplet.

44
Q

What is the forever amino acid attachment site on tRNA?

A

CCA.

45
Q

Where do Hydrogen bonds between paired bases in tRNA result?

A

3-dimensional structure.

46
Q

What does Aminoacyl tRNA synthase do?

A

It links each amino acid to its relative tRNA.

47
Q

What does the linking of amino acids to relative tRNAs need?

A

Energy: ATP.

48
Q

How is the bond between amino acids and relatives tRNAs characterised?

A

Unstable.

49
Q

What does the charged tRNA deliver?

A

The amino acid to the ribosome.

50
Q

What are ribosomes?

A

Very large.
Multi-protein.
Multi-RNA (rRNA).
Complexes.

51
Q

What are the differences between prokaryotic and eukaryotic ribosomes?

A

rRNAs sizes.

Main protein subunits.

52
Q

What does the ribosome tighten?

A

mRNA between smaller 30S subunit and larger 50S.

53
Q

Why does the ribosome tighten mRNA between large and small subunits?

A

To form the active structure.

54
Q

What does the 50S subunit of ribosome contains?

A

Sites:
A
P
E.

55
Q

What do the 3 sites of 50S subunit of ribosome bind?

A

Charged tRNAs.

56
Q

What does 50S subunit of ribosomes do once it binds to charged tRNAs?

A

It removes the amino acid –> adds it to the growing peptide chain.

57
Q

Where does the small ribosomal subunit bind?

A

To the mRNA.
At Shine-Dalgarno sequence.
–> special charged tRNA (fMet) in P site.

58
Q

What does the fMet/charged tRNA in P site recognise?

A

The translation start codon (ATG).

59
Q

By what is the charged tRNA delivered to the P site?

A

By EF-Tu.

60
Q

What do the new charged tRNAs recognise?

A

Their mRNA triplets.

61
Q

Where are the new charged tRNAs delivered?

A

To the A site.

62
Q

Where is the growing peptide held?

A

In the P site.

63
Q

Where is the growing peptide transferred?

A

To the new amino acid.

64
Q

How is the growing peptide transferred to the new amino acid?

A

In a shuffle-action along mRNA transcript.

65
Q

From where is the empty tRNA released?

A

From the E site.

66
Q

Why is the empty tRNA released form the E site?

A

To be re-used.

67
Q

Where does EF-G help?

A

In the translocation process.

68
Q

By what is the stop signal recognised in translation process?

A

By the Release factor.

69
Q

What does the Release factor do once it recognises the stop signal?

A

It binds to the A site –> releases peptide from P site.

70
Q

What happens to the ribosome after the new peptide is released?

A

It fall in small and large subunits.

Groups together at a new Shine-Dalgarno site on a new mRNA.

71
Q

How is the translation process characterised?

A

Central.
Complex.
Costly.
Heavily regulated at levels.

72
Q

How can sites on mRNA be hidden/uncovered?

A

By folding.

By RNA-binding proteins.

73
Q

Why are the sites of mRNA hidden/uncovered?

A

To prevent/initiate translation.

74
Q

Why can ribosomal subunits/other factors be targeted?

A

To control elongation/termination.

75
Q

What are the translation control points?

A

Antibiotic/antibiotic resistance targets.

Molecular Biology and Genetics (15 decks)

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