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Protein Synthesis And Protein Function- Exam III Flashcards

1
Q

Eukaryotic translation is driven by:

A

Ribosomes

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2
Q

What type of structure are ribosomes?

A

Multimeric

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3
Q

What rRNAs are involved in eukaryotic translation? (4)

A

28S
18S
5.8S
5S

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4
Q

Ribosomal machinery is assembled within the:

A

Nucleolus

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5
Q

What is unique about the nucleolus?

A

Not a membrane bound structure

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6
Q

What serves as guide RNAs to direct specific modifications of the rRNAs?

A

snoRNA (small nucleolar RNAs)

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7
Q

In eukaryotic translations, the modification on the 2-OH position of the nucleotide ribose sugar include:

A

~100 methylations of the 2-OH position

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8
Q

In eukaryotic translation, what modification occurs on uridine nucleotides creating psuedouridine?

A

~100 isomerizations

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9
Q

Ribosomes found in the cytosol (moving anywhere) - NOT found in nucleus and other organelles

A

Free ribosomes

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10
Q

If the protein being made contains an endoplasmic reticulum targeting sequences, then the ribosomes are associated with the:

A

Rough ER

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11
Q

Ribosomes associated with the rough ER are considered what type of ribosome?

A

Membrane bound ribosomes

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12
Q

There is a very specific _____ pathways associated with proteins made in the ribosome of the RER

A

Secretory pathways

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13
Q

What is read by the ribosomal machine as a triplet of sequential nucleotides (codon)

A

mRNA

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14
Q

Where does translation start?

A

5’ end of the mRNA

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15
Q

What do tRNAs have that basepair with the codons of mRNA

A

Anti-codon

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16
Q

TRNAs are “charged” by the addition of a specific _____ that corresponds to that codon.

A

Amino acid

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17
Q

The aminoacyl-tRNA is created by the action of enzymes called:

A

Aminoacyl-tRNA synthetases

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18
Q

Protein translation uses basepairing between:

A

The codon (in mRNA) and the anticodon (in tRNA)

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19
Q

There is a ____ for each codon, anticodon pair.

A

TRNA

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20
Q

Steps of translation:

A

Activation, initiation , elongation, termination

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21
Q

Step of translation: formation of aminoacyl-tRNAs

A

Activation

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22
Q

Step of translation: binding of ribosome to 5’end of mRNA and subsequent binding of initiator Met-tNA

A

Initiation

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23
Q

Step of translation: synthesis of the peptide chain

A

Elongation

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24
Q

Step of translation: synthesis stops and peptide is released from the ribosome

A

Termination

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25
The 3rd base of the anticodon triplet in the codon generates the wobble position and is generally the least important for:
Base pairing
26
Translation starts with AUG codon in the mRNA , which in about 90% of cases is the _____ in the mRNA
First AUG
27
Generally speaking how many stop codons are necessary to terminate translation?
2
28
A small ribosomal subunit attaches to the 5’ end of mRNA due to recognition of the:
5’cap structure
29
The small ribosomal subunit moves along the mRNA until it encounters the first methionine where _____ will bind.
Met-tRNA and the large ribosomal subunit
30
Aminoacyl tRNAs will bind the ____ site of the ribosome
A site (Aminoacyl- site)
31
The ribosome moves 5’ to 3’ along the mRNA. As the ribosome moves, the met-tRNA is simultaneously shifted to the ____ site.
P site (peptide site)
32
After the met-tRNA is shifted to the P site, the ____ is now open for the next aminoacyl-tRNA corresponding to the next codon to bind.
A- site
33
The process of translation largely uses what form of energy?
GTP
34
What type of bond is formed between the Met-tRNA and the new aminoacyl-tRNA in the A site.
Peptide bond
35
When peptide bond is formed between the Met-tRNA and the aminoacyl-tRNA , this forms a ____ in the A site and leaves and a ____ tRNA in the p-site
Dipeptide ; empty tRNA
36
Once the dipeptide is formed, leavening an empty tRNA in the p site, the ribosome then moves simultaneously discharging the empty tRNA and shifting the peptide into the:
P site
37
Once a stop codon is encountered, termination of the polypeptide chain involves ____ of the ester bond which release the protein.
Hydrolysis
38
Many antibiotics target:
Transcription or translation
39
Prevents RNA synthesis
Riamycin
40
Blocked the binding of the aminoacyl-tRNA to the A-site ( also binds newly forming mineralizing surfaces)
Tetracycline
41
Prevents the switch from translation initiation to elongation and can also cause protein miscoding
Streptomycin
42
Blocks the peptides transferase reaction so elongation is prevented
Chloramphenicol
43
Blocks the ribosome exit channel in the ribosome so elongation is inhibited
Erythromycin
44
What antibiotics have some type of mechanism dealing with elongation (translation step)
Streptomycin, chloramphenicol and erythromycin
45
Linear sequence of amino acids
Primary structure
46
Stretches in the polypeptide chain that form alpha helices and beta-pleated sheets
Secondary structure
47
What are the two forms of the beta-pleated sheet?
Anti-parallel Parallel
48
Changes in amino acids sequence can have a profound effect on:
Protein structure and function
49
The full 3 dimensional structure of a protein
Tertiary structure
50
Designation used for proteins that have multiple polypeptide chains (subunits) and refers to teh complete structure of all subunits.
Quaternary structure
51
Shared sequences of amino acids that can be used to identify potential members of a protein family
Protein motifs
52
Share protein motifs generally equate to:
Similar functions
53
Structural entities that function essentially independently within a protein
Protein domains
54
Protein domains can be build from:
Specific motif or set of motifs
55
A single protein can have _____motifs and domains
Multiple
56
Proteolytic enzyme cleavage sites and phosphorylation sites are examples of:
Protein sequence motifs
57
RGD sequence and heparin binding sites are examples of:
Binding motifs
58
Transmembrane spanning sequences and protein secretion leader sequences are examples of:
Protein sequence motifs
59
Many proteins have a _____ structure which also appears in other proteins. These structural motifs are formed by the 3D arrangement of amino acids nad do not necessarily predict a biological function
Supersecondary
60
What can be found in both proteins and DNA and generally have biological significance
Sequence motifs
61
Common in transcription factors and consists of alpha helices bound by a looping stretch of amino acids (motif)
Helix-loop-helix
62
DNA binding motif consisting of two alpha helices joined by a short stretch of amino acids
Helix-turn-helix
63
DNA binding motif consisting of two beta strands
Zinc finger
64
Alu, DNA transposing, LINE, SINE, SSRs, and etc. are all examples of:
DNA sequence repeat elements
65
The odontoblasts cells form:
Dentin
66
What are the cells derived from the dental papilla?
Odontoblasts & undifferentiated mesenchymal cells fibroblasts
67
What cells are derived from the dental follicle?
Cementoblasts, fibroblasts, osteoblasts
68
Odontoblasts give rise to:
Dentin
69
Undifferentiated mesenchymal cell fibroblasts give rise to:
Pulp
70
Cementoblasts give rise to:
Cementum
71
Fibroblasts give rise to:
Periodontal ligament
72
Osteoblasts give rise to:
Alveolar bone
73
What cells are derived from the inner dental epithelium
Ameloblasts
74
Ameloblasts give rise to:
Enamel
75
Major protein of enamel: that stabilizes the amorphous calcium phosphate phase, control of apatite crystal morphology and organization, and controls enamel thickness
Amelogenin
76
Amelogenins have the ability toe______ into nano sphere and thereby guid HAP crystal formation and growth.
Self-assemble
77
Major protein of enamel: cell adhesion protein, controls cell differentiation, and maintains rod integrity
Ameloblastin
78
Major protein of enamel: cooperates with amelogenin to control mineral nuclear ion and elongated growth
Enamelin
79
Major protein of enamel: Digests enamel proteins during maturation stage facilitating the removal and hardening the final layer of enamel
Kalikrein 4
80
Major protein of enamel: Cleaves amelogenin, ameloblastin and enamelin at the secretory stage to produce stable intermediates with defined functions
Mmp-20
81
What is formed by ameloblasts and contians 90% amelogenin and 10% enamelin.
Enamel
82
In enamel, as appetite crystals grown, ____ is removed:
Amelogenin
83
____ is high in proline, leucine, histidine, and glutamine, but contians no hydroxyproline of cystine.
Amelogenin
84
There are two genes for amelogenin, one on the X and the other on the Y chormosome which result in minor in enamel between males and females. The gene on the X is: The gene on the Y is :
AMELX AMELY
85
The self assembly of amelogenin is dependent upon:
Hydrophilic C-terminus
86
Occurs before the formation of enamel (reciprocal induction)
Dentin formation
87
Odontoblasts differentiate from cells in the:
Dental papilla
88
Secrete their organic matrix around the area that is directly adjacent to the inner enamel epithelium.
Odontoblasts
89
When odontoblasts move toward the center of the center of the tooth they form:
Odontoblasts process
90
Odontoblasts secrete _____ and mineralize matrix forming the mantle dentin
Hydroxy appetite crystals
91
What is the major component found in dentin?
Type I collagen
92
The small integrin-binding ligand N-linked glycoproteins
SIBLING family proteins
93
Immediately cleaved after secretion into DSP, DGP, and DPP
DSPP
94
Produced by odontoblasts and early-stage osteocytes
DMP1
95
Plays a role in biomineralization
Bone sialoprotein
96
HA binding and contains and RGD motif, mineralization inhibitor
Osteopontin
97
Matrix extracellular phosphoglycoprotein. Contains an RGD motif and in bone appears to be an inhibitor of mineralization
MEPE
98
Acellular cementum forms before ____
Cellular cementum
99
The periodontal ligament is formed by _____ cells of the dental follical
Fibroblast cells

Applied Biochem (18 decks)

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