Translation Flashcards

1
Q

How many possible codons are there?

A

64

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2
Q

What is a triplet binding assay?

A

A test which proves synthetic trinucleotides can promote binding of specific tRNAs to ribosomes.

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3
Q

How many sense codons are there?

A

61

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4
Q

Where is the code not universal?

A

In mitochondria

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5
Q

What is tRNA?

A

The adaptor between codons and amino acids.

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6
Q

How does the tRNA link to its amino acid?

A

Through covalent bonding.

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7
Q

What part of the tRNA recognises the codon?

A

The anticodon

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8
Q

What defines the cloverleaf structure of tRNA?

A

4 stems and 4 loops

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9
Q

What do the hydrogen bonds between paired bases of the tRNA result in?

A

Its 3D structure

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10
Q

What is the open reading frame?

A

The protein coding sequence in a gene.

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11
Q

What is meant by the genetic code being degenerate?

A

Most amino acids have more that one codon.

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12
Q

What happens to the tRNA when it binds the amino acid?

A

It becomes charged

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13
Q

How does the tRNA associate with the mRNA molecule?

A

Through the anticodon loop

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14
Q

What is the function of aminoacyl-tRNA synthetase?

A

It catalyses the covalent linkage between the 3’ end of the tRNA and its cognate amino acid.

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15
Q

Which tRNAs does aminoacyl-tRNA synthetase recognise?

A

All isoaccepting tRNAs

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16
Q

How many aminoacyl-tRNA synthetases are there?

A

One per amino acid

17
Q

What did Seymour Benzer discover?

A

That protein synthesis machinery recognises the anticodon not the amino acid associated with the tRNA.

18
Q

What led Seymour Benzer to their discovery?

A

A cysteine charged tRNA was chemically changed to become an alanine charged tRNA. Alanine was then incorporated into the polypeptide chain instead of cysteine.

19
Q

What parts of translation are subject to proofreading?

A

Amino acid selection and tRNA selection.

20
Q

What is the process of kinetic proofreading?

A

If the wrong amino acid is selected the forward reaction is disfavoured and so slows.

21
Q

What is the process of chemical proofreading?

A

If the wrong amino acid is selected the catalytic reaction is reversed.

22
Q

What does proofreading avoid?

A

The need for absolute accuracy.

23
Q

What do sticky mutations result in in mice?

A

A neurodegenerative disease

24
Q

At what loci were sticky mutations found?

A

In the AlaRs gene encoding alanyl-tRNA synthetase.

25
What can a defect in proofreading lead to?
A higher level of ser-tRNA ala synthesis (mis charging with serine)
26
How many tRNA molecules are there?
Around 30
27
What allows one tRNA to decode more than one codon?
Wobble and modified bases.
28
What is the wobble hypothesis?
Watson-Crick base pairing rules between anticodon position one and codon position three are relaxed due to flexibility and modifications of the anticodon loop.
29
What is the structure of ribosomes?
It consists of two subunits. The larger subunit has three rRNA molecules and 49 different proteins in a precise pattern. The smaller subunit has one rRNA and 33 proteins.
30
How are ribosomal subunits held together?
By ionic and hydrophobic forces.
31
What forms the bulk of RNA structure in bacteria?
The 50s crystal
32
What fills the gaps between rRNA?
Proteins
33
What catalyses peptide bond formation?
The 23s rRNA (ribozyme)
34
How many tRNA binding sites are there on the largest ribosome subunit?
Three
35
Where do codon-anticodon interactions between tRNA and mRNA occur?
At the P and A sites
36
What is the function of the A (aminoacyl tRNA/entry) site?
It binds the anticodon to the charged tRNA.
37
What is the function of the P (peptidyl tRNA/donor) site?
It is where the tRNA adds the amino acid to the growing peptide chain.
38
What is the function of the E (exit) site?
It is where the tRNA sits before being released from the ribosome.
39
What are the stages of translation?
Initiation, elongation and termination