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MCM test 2 > Genetics > Flashcards

Genetics Flashcards

1
Q

Genetic Code

A

‘rules’ that convert the nucleotide sequence of a gene to a sequence of amino acids of a protein using mRNA as an intermediary

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2
Q

Degenerate Code

A

some amino acids can be coded by more than one codon and 3 codons are STOP codons

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3
Q

Silent Mutation

A

doesn’t change the amino acid

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4
Q

Missense Mutation

A

Changes amino acid in the protein with no effect on protein function

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5
Q

Nonsense Mutation

A

Codon changes to a stop codon

  • causing premature chain termination
  • protein is formed as a truncated version
  • Protein is non-functional
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6
Q

Frameshift Mutation

A

One or more nucleotides are depleted or inserted into ORF, which causes a change in the codon sequence and a change in the amino acid sequence
*Protein is non-functional

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7
Q

Sickle Cell Anemia

A

missense mutation

  • changes Val (hydrophobic) to Glu (-charged+hydrophil)
  • changes in conformation of HbA: aggregate, rigid, rod-like structures
  • deformed RBCs with poor oxygenation and clogs capillaries
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8
Q

Duchenne Muscular Dystrophy

A
  • deletion in the dystrophin gene leading to partial or non-functional dystrophin protein
  • OOF deletions give little/no expression of dystrophin protein
  • muscle wasting
  • frame shift deletions–truncated forms of dystrophin
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9
Q

mRNA

A
  • 5’ cap
  • -untranslated region
  • -Coding region
  • -3’untranslated region
  • Poly A tails
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10
Q

tRNA

A
  • serves as adaptors
  • binding site for codons and amino acids
  • match amino acids to codons in mRNA
  • Clover leaf (2dry structure)
  • Anticodon loop
  • 3’CCA terminal region
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11
Q

3’ CCA terminal region

A

found in tRNA

-binds the amino acid that matches the corresponding codon

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12
Q

Anticodon loop

A

found in tRNA

-set of three consecutive nucleotides that pair with a complementary codon in mRNA

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13
Q

Aminoacyl tRNAs

A

(tRNA with amino acid)

  • AA needs to be activated
  • catalyzed by aminoacyl tRNA synthetases which serves as a second genetic code
  • each tRNA is charged with the correct AA to maintain fidelity of protein synthesis
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14
Q

Activation of Amino Acids

A
  1. Aminoacyl tRNA synthetase catalyzes the addition of AMP to the carboxy end of AA
  2. the AA is transferred to the cognate tRNA
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15
Q

Ribosomes

A

assemblers of translational machinery

  • large complexes of proteins and rRNA (L+S subunit)
  • antibiotics are used to target prokaryotic translational machinery
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16
Q

Ribosomal Complex

A
  • Acceptor site
  • Peptidyl site
  • Empty/Exit site
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17
Q

Acceptor Site

A

(on ribosome)

-mRNA codon exposed to receive aminoacyl tRNA

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18
Q

Peptidyl Site

A

(on ribosome)

-where aminoacyl tRNA is attached

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19
Q

Empty/Exit Site

A

(on ribosome)

-location occupied by empty tRNA before exiting the ribosome

20
Q

Translation

A

5’ to 3’

  • Initiation
  • Elongation
  • Termination
21
Q

Initiation

A

(translation)
formation of mRNA, which is a small ribosomal subunit and initiator tRNA pre-initiation complex

-requires the hydrolysis of 1 GTP

22
Q

Elongation

A

(translation)
-activated AA attached to initiating Methionine by forming a peptide bond

*requires the hydrolysis of 2 GTP per amino acid added

23
Q

Termination

A

(translation)

  • peptide chain is released from ribosomal complex
  • requires hydrolysis of 1 GTP
24
Q

Peptidyl transferase

A

(translation)

- catalyzes peptide bond formation between amino acid in A and P site

25
Q

5’ cap

A

mRNA

-7 methyl guanasine cap

26
Q

Streptomycin

A

binds 30s subunit to disrupt initiation of translation

27
Q

Shigatoxin

A

binds to 60s subunit to disrupt elongation

28
Q

Clindamycin/Erythromycin

A

bind 50s subunit to disrupt translocation of ribosome

29
Q

Tetracyclines

A

bind 30s subunit to disrupt elongation

30
Q

Peptidyl Transferase

A

housed in the large subunits of the ribosome

31
Q

Diptheria Toxin

A

inactivates EF2-GTP and inhibits elongation

32
Q

Prokaryote Ribosome

A

50s subunit and 30s subunit

33
Q

Eukaryotic Ribosome

A

60s subunit and 40s subunit

34
Q

Mitochondria Proteins

A

contain an N terminal hyrophobic alpha helix

have TOM or TIM to signal for peptide import

35
Q

Nucleus Proteins

A

Rich in Lysine and Arginine

36
Q

Peroxisome Proteins

A

have an SKL sequence (cytosolic pathway)

37
Q

Endoplasmic Reticulum Proteins

A

Secretory Pathway

  • go to ER first
  • have an ER ‘retention signal’ with amino terminus (positive charge)
38
Q

KDEL

A

Endoplasmic Reticulum ER retention signal

39
Q

Lysosomal Proteins

A

have a mannose 6 phosphate signal from secretory pathway…go to ER first

40
Q

Secretory Proteins

A

have Tryptophan rich domains…from secretory pathway that hit the ER first

41
Q

Heat Shock Proteins

A

protect the unfolded proteins that are entering the mitochondria via the TOM and or TIM

42
Q

SRP

A

Signal Recognition Particle–brings together the ER membrane and the ribosome

43
Q

I-Cell Disease

A

lysosomal storage disorder to the defective tagging of lysosomal proteins with Mannose-6-Phosphate so there is an increase is plasma lysosome levels

44
Q

Chaperone Proteins

A

needed by large proteins for protection and folding guidance into proper tertiary structure to avoid aggregation and proteolysis

45
Q

Chaperonins

A

barrel shaped compartments that admit unfolded proteins and catalyze folding in an ATP dependent manner

46
Q

Glycosylation

A

PTM

  • O linked form in a serine residue
  • N linked form in Asparagine

*cataract formation

47
Q

Post-Translational Modification of Collagen

A

Modification is important to collagen
Ascorbic acid is necessary for lysyl and proyxl hydroxylases and defects in this enzyme result in disorders such as Erlhers Danlos

MCM test 2 (3 decks)

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