Lecture 1.11 Flashcards

1
Q

Why is the genetic code considered degenerate?

A

There are multiple codons for some amino acids, thus there are more codes than it needs

-61 codons for 20 amino acids

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2
Q

What is wobble base pairing?

A

5’ position of the anticodon tolerates mismatches or non-standard base pairing

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3
Q

Nonsense mutation

A

Change an amino acid to a stop codon

  • terminates protein prematurely
  • almost always alters protein function
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4
Q

missense mutation

A

Change an amino acid due to a base change

  • allows protein synthesis
  • doesn’t always alter protein function
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5
Q

What are two sources of specificity in formation of aminoacyl-tRNAs?

A
  • high specificity

- tRNA synthetases have editing activity (hydrolyase)

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6
Q

What are three peptide binding sites in a ribosome and what is their function?

A

E-site: things exit the ribosome
P-site: growing polypeptide chain located here (also where the intiation complex attaches)
A-site: incoming tRNAs bind here

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7
Q

What are the general steps in translation initiation?

A
  • protein synthesis initiates at AUG (met) codon
  • specialized methionine tRNA binds to small subunit of ribosome (in the P-site)
  • small subunit binds to cap of mRNA and treks along until it encounters the first AUG codon
  • eIFs dissociate and large subunit binds
  • aminoacyl-tRNA binds to A site and first peptide bond forms
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8
Q

Steps of elongation

A
  • nascent polypeptide in P-site and a new aminoacyl-tRNA binds to the A-site
  • New peptide bond is formed by peptidyl transferase (ribozyme) and conformationals change causes the tRNA to move to the E- and P- sites
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9
Q

steps of termination?

A
  • stop codons mar the end of translation
  • release factors bind to ribosomes wit top codon in A-site
  • release factor causes peptidyl transferase to hydrolyze the last amino acid releasing the completed protein and resulting in disassociation of the ribosome
  • release factors are proteins that are shaped like a tRNA
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10
Q

How much energy is utilized to synthesize a peptide bond in a protein?

A

4 high energy bonds per every new peptide bond

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11
Q

Where is the energy needed to synthesize a peptide bond consumed in the cell?

A
  • 2 phosphate bonds cleaved from ATP –> AMP to charge the tRNA (put amino acid on tRNA)
  • 1 phosphate bond cleaved from GTP –> GDP to dissociate the initiation factors and allow the large ribosomal subunit to bind to the initiation complex
  • 1 phosphate bond cleaved from GTP–> GDP to translocate the mRNA and tRNA
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12
Q

suppressor

A

mutated tRNA

  • Nonsense suppressor: mutated anticodon complements terminator sequence (can inhibit effects of nonsense mutation
  • Frameshift suppressor: anticodon contains 4 residues and can insert an amino acid and restore a frame sift mutation
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13
Q

What differences in initiation of translation allow prokaryotes but not eukaryotes to have polycistronic mRNA?

A
  • Prokaryotic ribosomes can bind at any ribosome-binding site (rbs - which is upstream from AUG) on the mRNA and start protein translation of multiple proteins in a single mRNA
  • Eukaryotic ribosomes must attached at the 5’ cap
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14
Q

What is RNA editing ?

A

the modification of RNA after synthesis: modification of bases to change “meaning” of message

-molecular process through which some cells can make discrete changes to specific nucleotide sequences within an RNA molecule after it has been generated by RNA polymerase.

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15
Q

what is nonsense-mediated mRNA decay?

A

a pathway that acts on transcripts right after splicing to degrade RNAs containing nonsense mutations

-a surveillance pathway that exists in all eukaryotes. Its main function is to reduce errors in gene expression by eliminating mRNA transcripts that contain premature stop codons.

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16
Q

How are expression of ferritin and transferrin receptor regulated? (ferritin stores iron and transferrin help cells take up iron)

A
  • regulated by translational repression and mRNA stability
  • low iron levels = aconitase binds to both ferritin and transferrin receptor mRNA –> thus inhibiting ferritin and stabilizing transferrin
  • high iron levels = aconitase binds iron and realeases both messages –> thus increasing translation of ferritin and destabilizing transferrin
17
Q

What is the function of molecular chaperones in cells?

A

to help proteins fold properly and reach their final conformation
- require ATP hydrolysis to function

18
Q

What is the role of ubiquitin in protein turnover?

A

a small, highly conserved protein that is used as a signal for protein degradation

1) activated by E1
2) E1 binds to ubiquitin ligase complex (E2 & E3)
3) E3 binds to target protein
4) ubiquitin gets transferred to nitrogen termianl of protein

19
Q

hsp70-like chaperone

A

binds to hydrophobic patches on proteins (as they are prevalent if protein is improperly folded) and “slows” the initial folding

20
Q

hsp60-like chaperone

A

bind incorrectly folded proteins and creates a hydrophobic chamber ( a favorable environment for folding)

21
Q

Proteosome

A

protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases

22
Q

genetic code

A
  • has three residue words in a non-overlapping syntax
  • encodes 20 amino acids including 1 star codon and 3 stop codons
  • no punctuation
  • all nucleic acids have 3 reading frames
23
Q

Open reading frame

A

series of codons without stop codons

- reading frame that can be translated in a protein because it is long enough

24
Q

tRNA

A

short RNAs containing three step loops that form an L shaped structure
- 3’ end is linke to an amino acid and the anticodn loop base pairs with corresponding codon

25
Q

silent mutation

A

mutation that causes no change in the amino acid sequence due to the degenerate genetic code