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Biochem IV > Processing > Flashcards

Processing Flashcards

1
Q

Is eukaryotic mRNA monocistronic or polycistronic?

A

monocistronic

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2
Q

What type of RNA contains inosine? What can inosine bind to?

A

tRNA

A, C and U

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3
Q

What is the function of aminoacyl-tRNA synthetases?

A

to link tRNAs for their amino acid

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4
Q

80S?

A

human, cytosolic

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5
Q

55S?

A

human, mitochondrial

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6
Q

70S?

A

bacteria

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7
Q

What is the first tRNA beginning protein translation?

A

tRNA-met

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8
Q

What is eIF2a activated by?

A

GTP

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9
Q

What binds tRNA-met? What is this complex called?

A

eIF2a-GTP

ternary complex

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10
Q

What does the ternary complex bind?

A

small ribosomal subunit

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11
Q

What binds to the small ribosomal subunit?

A

mRNA

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12
Q

What marks the transition between the pre-initiation complex to the initiation complex?

A

binding of a large ribosomal subunit and GTP hydrolysis

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13
Q

When does elongation begin?

A

once tRNA-met binds to the P site

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14
Q

Where does the second amino acid go? WHat places it there? What provides the energy for this process?

A

E-site

EF-1

GTP

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15
Q

What protein aids the ribosome in moving one codon of the mRNA?

A

EF-2

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16
Q

The uncharged tRNA leaves the ribosome at what site?

A

E-site

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17
Q

What is the one amino acid a stop codon can code for?

A

selenocysteine

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18
Q

What protein pairs with a stop codon in the A site?

A

eukaryotic release factor

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19
Q

What is hydrolyzed on eRF to terminate translation?

A

GTP

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20
Q

How does streptomycin inhibit bacterial growth?

A

inhibits bacterial ribosome small unit and inhibits initiation

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21
Q

How do both neomycin and gentomycin function?

A

by causing mistranslation of codons

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22
Q

How does tetracycline function?

A

binds in A site.

inhibits tRNA binding

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23
Q

What is the MOA of chloramphenicol?

A

prevents peptidyl bond formation

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24
Q

How does ricin work?

A

removes adenine bases from rRNA large subunit

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25
Q

How does diptheria toxin function?

A

inactivates EF-2 by ADP-ribosylation

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26
Q

What two mechanisms are used to regulate translation?

A

preventing recognition of start codon

regulating activity of initiation factors

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27
Q

Chaperones bind to what region of nascent polypeptides?

A

hydrophobic

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28
Q

Where are chaperones concentrated in regards to their location?

A

cytosol and ER

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29
Q

Heat Shock Proteins are implicated in what disease?

A

Charcot Marie Tooth Disease

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30
Q

Where are exported proteins synthesized?

A

ER

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31
Q

Is the signal sequence hydrophilic or hydrophobic?

A

hydrophobic

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32
Q

What binds the signal sequence?

A

signal recognition particle (SRP)

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33
Q

Where does the SRP take the nascent polypeptide? What protein does it transger the polypeptide to?

A

ER membrane

translocon

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34
Q

What happens to the SRP after the nascent polypeptide has been transferred to the translocon?

A

dissociates

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35
Q

Where does the translocon transfer the nascent polypeptide?

A

from the cytosol to the ER

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36
Q

What cleaves the signal peptide?

A

a signal peptidase

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37
Q

What can trigger the unfolded protein response?

A

environmental responses

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38
Q

What is the unfolded protein response?

A

accumulation of unfolded proteins in the ER

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39
Q

What two types of proteins are often glycosylated?

A

excreted proteins and cell surface proteins

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40
Q

What donates the sugar for a glycosylated protein?

A

activated sugar nucleotide

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41
Q

What three tenets are glycosyltransferases specific for?

A

sugar donar, aceptor molecule, type of bond formed

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42
Q

Where are N-linked sugars attached?

A

asparagine

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43
Q

Where does N-linked glycosylation begin?

A

as protein emerges into the ER

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44
Q

What is the function of dolichol phosphate?

A

serves as a substrate for the genesis or a universal oligosaccharide

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45
Q

What is the first sugar to be transferred to asparagine during N-linked glycosylation?

A

universal oligosaccharide

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46
Q

Where does modification of the universal oligosaccharide occur?

A

golgi

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47
Q

What two types of protein are yielded following oligosaccharide trimming?

A

high mannose content and complex

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48
Q

Does N-linked glycosylation occur as the protein is being folded or after?

A

while the protein is being folded

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49
Q

When does O-linked glycosylation occur?

A

only after the protein has been folded

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50
Q

Where does O-linked glycosylation occur?

A

Golgi

51
Q

What residues can be O-linked glycosylated?

A

serine of threonine

52
Q

What is the first sugar to be transferred during O-linked glycosylation?

A

N-acetyl-galactosamine

53
Q

What are common examples of O-linked glycosylation?

A

blood group antigens

54
Q

The A allele possesses what sugar?

A

N-acetyl-galactosamine

55
Q

The B allele possesses what sugar?

A

galactose

56
Q

What is the disease process in multiple sulfatae deficiency?

A

failure to convert cysteine to formylglycine

57
Q

Patients with MSD present with what type of symptoms?

A

mucopolysaccharidoses

58
Q

What is always the first amino acid to be incorporated into a protein?

A

methionine

59
Q

What three hydrophobic molecules can be added to proteins?

A

palmitic acid, myristic acid isoprenoids

60
Q

What residue is myristic acid attached to?

A

glycine at N-terminus

61
Q

What residue to palmitic acid attached to?

A

cysteine residues throughout protein

62
Q

What residue are isoprenoids attached?

A

cysteine residues at c-terminus of protein

63
Q

Where are proteins phosphorylated to be destined for the lysosome?

A

mannose residues

64
Q

What donates the phosphate for phosphorylation of mannose?

A

N-acetyl-glucosamine

65
Q

What targets proteins to the lysosome?

A

Mannose-6-phosphate

66
Q

What targets proteins to the mitochondria?

A

presequence

67
Q

Where is this presequence located?

A

N-terminally

68
Q

What proteins mediate a protein containing a presequence into the mitochondria?

A

TOM and TIMs

69
Q

What are two energy intensive muscles?

A

nerves and mitochondria

70
Q

What causes Deafness-dystonia syndrome?

A

defective TIM protein

71
Q

Where is defective CFTR protein moved?

A

cytosol and degraded

72
Q

In I-cell disease, what two conditions can be detected?

A

dense inclusion bodies in fibroblasts

lysosomal proteins in the serum

73
Q

What kind of degradation process takes place in the lysosome?

A

non-specific degradation

74
Q

What other cellular process is the lysosome implicated in?

A

autophagy

75
Q

What type of degradation occurs in the proteasome?

A

specific degradation

76
Q

Addition of what protein targets a protein for proteasomal degradation?

A

ubiquitin

77
Q

How many units of ubiquitin are transferred?

A

multiple

78
Q

What is the function of E1?

A

activate ubiquitin

79
Q

What protein is ubiquitin conjugated to before being added to proteins?

A

E2

80
Q

What protein conjugates ubiquitin to proteins?

A

E3

81
Q

What else does E3 do?

A

identifies proteins for ubiquitination

82
Q

What specifically targets a protein for proteasomal degradation?

A

poly-ubiquitination

83
Q

What two amino acids at the N-terminal signal for a short life span?

A

Arg or Lys

84
Q

What two amino acids at the N-terminal signal for a longer life span?

A

Met or Ser

85
Q

What tetramer sequence signals for a short life-span of a protein?

A

PEST sequence

86
Q

What base is contained in tRNA that is not contained in other RNAs?

A

inosine

87
Q

What protein attaches an amino acid to a tRNA?

A

aminoacyl-tRNA synthetases

88
Q

How does streptomycin function?

A

inhibits initiation

89
Q

How do neomycin and streptomycin function?

A

cause mistranslation of codons

90
Q

What does ricin do to rRNA?

A

removes adenine bases

91
Q

What does diptheria toxin inhibit? How does it do this?

A

inhibits EF-2

ADP ribosylation

92
Q

What binds the signal sequence of a protein?

A

signal recognition particle (SRP)

93
Q

What is the function of the translocon?

A

to transfer a nascent protein from cytosol to the ER

94
Q

What signals the unfolded protein response?

A

accumulation of unfolded proteins in the ER

95
Q

What two types of proteins are glycosylated?

A

proteins to be excreted and cell surface proteins

96
Q

Where does glycosylation begin? Where does it continue?

A

ER

Golgi

97
Q

During N-linked glycosylation, where does modification of the univeral oligosaccharide occur?

A

golgi

98
Q

Where does O-linked only occur? What type of proteins is O-linked occuring?

A

only golgi

only fully formed proteins

99
Q

What is transferred to proteins during O-linked glycosylation?

A

N-acetyl-galactosamine

100
Q

What type of cells commonly express O-liknked proteins?

A

blood cell antigens

101
Q

What is added to the antigen of the A allele?

A

N-acetyl-galactosamine

102
Q

What is added to the antigen of the B allele?

A

galactose

103
Q

What residue is myristic acid added to?

A

glycine

104
Q

What residue is palmitic acid added to?

A

cysteines throughout

105
Q

What residue are isoprenoids added to?

A

cysteines as C-terminus

106
Q

What is the function of a GPI anchor?

A

anchor proteins to external surface of plasma membrane

107
Q

What serves as the phosphate donor for mannose?

A

N-acetyl-glucossamine

108
Q

Deafness-Dystonia disorder is caused by a mutation in what protein?

A

TIM protein

109
Q

What two cellular happenings can one see with I-cell disease?

A

lysosomal proteins in the serum

inclusion bodies on fibroblasts

110
Q

Other than non-specific degradation of proteins, what else can the lysosomes be involved in?

A

autophagy

111
Q

What is the function of the E1 proteins?

A

activate ubiquitin

112
Q

What is the function of the E3 proteins?

A

ligate uiquitin to proteins

113
Q

Proteins with what two N-terminal residues are unstable?

A

arginine or lysine

114
Q

What particular tetramer shortens the life-span of proteins?

A

PEST

115
Q

What is a congenital disease involving protei chaperones?

A

Charcot Marie Tooth Disease

116
Q

What is CDG-1?

A

defective production of lipid linked oligosaccharide

117
Q

What is CDG-2?

A

defective trimming of oligosaccharide tree

118
Q

What is the first sugar added in O-linked glycosylation?

A

N-acetylgalactosamine

119
Q

What are two examples of O-linked glycosylated proteins?

A

proteoglycans and blood group antigens

120
Q

What sugar does the A antigen possess?

A

N-acetylgalactosamine

121
Q

What sugar does the B antigen possess?

A

galactose

122
Q

Where is the GPI anchor added? What is its purpose?

A

GPI anchor added at C-terminus

to tether proteins to external side of C-terminus

123
Q

What two residues is the ubiquitin bond formed between?

A

glycine and lysine

Biochem IV (6 decks)

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