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MCM- Exam 2 > Protein Processing > Flashcards

Protein Processing Flashcards

1
Q

What is DNA to RNA called

A

Transcription

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2
Q

What is RNA to protein called

A

Translation

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3
Q

What is the start codon

A

AUG; methionine

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4
Q

What are the four different mutations

A

Silent
Missense
Nonsense
Frameshift

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5
Q

What does a silent mutation cause

A

does not change the AA

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6
Q

What does a missense mutation cause

A

Changes AA in the protein, with either positive or negative effect

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7
Q

What does a nonsense mutation cause

A

Codon changes into a stop codon; and the protein is truncated

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8
Q

What does a frameshift mutation cause

A

One or more nucleotides are deleted or inserted

Change the codon and the rest of the codons in the sequence

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9
Q

What is the AA mutation in Sickle Cell Anemia

A

Missense mutation of Glutamic Acid to Valine

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10
Q

What is Sickle Cell Anemia

A

Aggregate and form rigid, rod-like structures in the RBC’s.

RBC’s have poor oxygen capacity and tend to clog capillaries

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11
Q

What is the mutation in Duchenne Muscular Dystrophy

A

Frameshift

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12
Q

What is the worst mutation in Duchenne Muscular Dystrophy

A

Out-of-Frame shift

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13
Q

What does the mRNA have on its 5’ side

A

7-methlyguanosine cap

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14
Q

What does the mRNA have on its 3’ side

A

Poly-A Tail

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15
Q

What does the Poly-A Tail do

A

Protect the mRNA from degradation

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16
Q

What does the 7-methyl guanosine cap do

A

Protection

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17
Q

What is the translator from mRNA to Amino Acids

A

tRNA

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18
Q

What is an Aminoacyl tRNA

A

A tRNA with an Amino Acid

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19
Q

What does an Aminoacyl tRNA synthetase do

A

catalyze the addition of AMP to COOH end of the Amino Acid; brings the correct tRNA to the mRNA to form peptide bonds

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20
Q

What is the make up of a Eukaryote Ribosome

A

60S Large Unit

40S Small Unit

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21
Q

What is the make up of a Prokaryotic RIbosome

A

50S Large unit

30S Small Unit

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22
Q

What is the A site of the Ribosome Complex

A

The acceptor site where new tRNA come in to elongate the peptide

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23
Q

What is the P site of the Ribosome Complex

A

Where Methionine binds to begin translation

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24
Q

What is the E site of the Ribosome Complex

A

Where the tRNA translocates out of the complex so that more can come in

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25
Q

What is the first step of Initiation

A

The 40S sub-unit binds Methionine

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26
Q

What is the Elongation step

A

tRNA’s bind at the A site and then translocate to the P site, to form a peptide bond between the AA’s

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27
Q

What are the stop codons

A

UAA, UAG, and UGA

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28
Q

What is the Termination Step

A

The peptide Chain is cleaved from the ribosomal complex. The release factors bind to the A site and cleave the ester bond between the C terminus of the polypeptide and the tRNA. GTP Hydrolysis splits the 60S and 40S sub-units

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29
Q

What do Polysomes do

A

Make protein synthesis more efficient

30
Q

What does Streptomycin Binds

A

The 30S subunit to disrupt the initiation of translation

31
Q

What does Shiga Toxin Bind

A

The 60S subunit to disrupt elongation

32
Q

What do Clindamycin and Erythromycin bind

A

the 50S subunit to disrupt translocation of the ribosome

33
Q

What do Tetracyclines bind

A

The 30S Subunit to disrupt elongation

34
Q

Where is Peptidyl transferase housed

A

In the large subunits

35
Q

What does the Diptheria Toxin Bind

A

Inactivates EF2-GTP and inhibits elongation

36
Q

What are the Prokaryotic Elongation Inhibitors

A

Tetracycline, Chloramphenicol, Clindamycin, Erythromycin, and Streptomycin

37
Q

What does Chloramphenicol do

A

inhibits peptidyl transferase in Prokaryotes

38
Q

What are the Eukaryotic Elongation Inhibitors

A

Cycloheximide, Diptheria Toxin, Shiga Toxin

39
Q

What does Cycloheximide do

A

Inhibits peptidyl transferase in Eukaryotes

40
Q

What is an Elongation inhibitor

A

Puromycin

41
Q

What does an Elongation Inhibitor do

A

Causes premature chain termination in Eukaryotes and Prokaryotes

42
Q

What are the two protein sorting pathways

A

Cytoplasmic and Secretory

43
Q

Where does the Cytoplasmic pathway go

A

Cytosol, Mitochondria, Nucleus, and Peroxisomes

44
Q

Where does the Secretory Pathway go

A

ER, lysosome, plasma membrane, or for secretion

45
Q

What is the tag for the cytoplasmic pathway

A

Nothing

46
Q

What is the tag for the mitochondria

A

N terminal hydrophobic alpha-helix

47
Q

What are the two transporters inside the Mitochondria

A

TIM and TOM; the transporter of the inner membrane and the transporter of the outer membrane. Have to go through TOM, not necessarily TIM

48
Q

What protects the proteins going into the Mitochondria

A

Heat Shock Proteins 70

49
Q

What is the tag for large proteins into the Nucleus

A

Four continuous basic residues (Lys and Arg)

50
Q

How are the proteins imported into the Nucleus

A

Nuclear Pores

51
Q

How do small proteins pass into the Nucleus

A

Small proteins able to pass through specific pores

52
Q

What is the tag for Secretory pathway

A

N-Terminal Positive Charge; to go to the ER

53
Q

What is the tag for the ER Protein

A

K-Lysine, D-Aspartic Acid, E-Glutamic Acid, L-Leucine

54
Q

What is the tag for Lysosomal Proteins

A

Mannose-6-phosphate

55
Q

What is the tag for Membrane Proteins

A

N Terminal apolar region

56
Q

What is the tag for proteins that get secreted through the Secretory Pathway

A

Tryptophan Domain

57
Q

What is a signal recognition particle

A

binds to the ER-targeting signal and the ribosome during translation

58
Q

What does the SRP do

A

wraps itself around ribosome-mRNA-peptide complex, tethering it to the ER membrane and halting translation temporarily

59
Q

Why does the SRP halt translation

A

To Post-Translationaly alter the protein towards their final destination

60
Q

What is I-Cell disease

A

Tagging of lysosomal proteins with Mannose 6-P is defective

61
Q

What happens in I-Cell disease

A

The lysosome cant get the proteins necessary to breakdown stuff
Just pretty much fucks you up

62
Q

What do chaperone proteins do

A

Help fold larger protein

63
Q

Post Translation Modifications (4)

PTM

A

Acetylation
Glycosylation
Phosphorylation
Disulfide Bonds

64
Q

What is Acetylation PTM

A

Covalent Linkage to Amine; happens to Lysine

HATs and HDACs

65
Q

What is Glycolysation PTM

A

O-Glycolysation; Hydroxyl bond, Serine and Threonine

N-Glycolysation; Acid Amide bond, Asparagine and Glycine, Asparagine mostly

66
Q

What is Phosphorylation PTM

A

Phosphate linked via esterification; Serin, Tyrosine, Threonine, Asparagine, and Histidine
Kinase adds
Phosphatase detracts

67
Q

What is Disulfide Bond PTM

A

Oxidation to achieve covalent linkage of Cysteine residues; Cysteine
Inter or Intra molecular

68
Q

What is Alzheimers Disease

A

Beta-Amyloid Plaque build up extracellularly

Hyperphosphorylation of Tau forming neurofibrillary tangles intracellularly

69
Q

What is Parkinson’s Disease

A

Aggregation of alpha-synuclein forming Lewy bodies in dopaminergic neurons in the substantia nigra
Dopamine deficiency

70
Q

What is Huntington’s Disease

A

Mutation in the Huntington Gene results in expansion of CAG triplet repeats; resulting in polyglutamine repeats
Misfold and aggregate
Selective death of cells in basal ganglia cause symptoms

71
Q

Creutzfeldt-Jakob Disease

A

Spongiform Encephalopathy
Caused by misfolding proteins, called prions
Transmissable

MCM- Exam 2 (3 decks)

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