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WorksheetsGenomics Exam 2
Total questions: 95
Worksheet time: 53mins
In Prokaryotes, the ribosome has 2 subunits, ___S + ___S = ___S
(Don't put any markings in answer [e.g. 20 30 40 if it was 20+30=40])
(a)
In Eukaryotes, the ribosome has 2 subunits, ___S + ___S = ___S
(Don't put any markings in answer [e.g. 20 30 40 if it was 20+30=40])
(a)
Which site of the ribosome is the exit site?
E
P
A
Z
Which site of the ribosome is the peptidyl binding site?
A
P
E
Z
White site of the ribosome is the aminoacyl binding site?
A
P
E
Z
What are the 2 functions of tRNA Synthetase?
Synthesis
Editing
Folding
Splicing
What is the function of the synthesis site in tRNA Synthetase?
Synthesis
Editing
Splicing
Deleting
What is the function of the editing site in tRNA Synthetase?
Synthesis
Proofreading
Folding
Ejection
What type of bond links tRNA to an amino acid?
Ester
Peptide
Ionic
Sulfide
What part of tRNA does an amino acid bind to?
Hydroxyl
Hairpin
Anticodon
Cap
What is the function of IF-1 in prokaryotic translation initiation?
Prevent aminoacyl-tRNA binding
Facilitate aminoacyl-tRNA binding
Stabilize 30S subunit
Prevent 50S subunit binding
What is the function of IF-3 in prokaryotic translation initiation?
Facilitate aminoacyl-tRNA binding
Stabilize 30S subunit
Prevent 50S subunit binding
Facilitate 50S subunit binding
What is the role of IF-2 in prokaryotic translation?
binds to fMet-tRNA
binds to tRNA
prevents fMet-tRNA binding
prevents tRNA binding
Which site does the start codon first bind to in the 30S subunit in prokaryotic translation?
A
P
E
Z
Which molecule is hydrolyzed prior to 70S initiation complex becoming fully formed?
ATP
GTP
What's the function of EF-Tu in prokaryotic elongation?
Transferring aminoacyl-tRNA into the A site
Transferring aminoacyl-tRNA into the P site
Transferring peptidyl-tRNA into the A site
Transferring peptidyl-tRNA into the P site
How does EF-Tu proofread?
Incorrect base pairs preferentially dissociate
Incorrect base pairs are ejected via an ATP-dependent mechanism
Incorrect base pairs are ejected via a GTP-dependent mechanism
Another enzyme performs proofreading on EF-Tu
Which enzyme catalyzes the amino acid peptide bond of the growing protein?
peptidyl transferase
peptidyl synthase
peptidyl esterase
peptidyl decarboxylase
Where is peptidyl transferase located?
Attached to the ribosome
Directly outside of the E site
Internally of the rRNA
It doesn't exist
Which enzyme translocates the tRNA inside of the ribosome?
EF-G
EF-Tu
EF-alpha
EF-beta
Which site will be the FIRST to recognize a stop codon in prokaryotes?
A
P
E
Z
What is leaky scanning?
A skipped stop codon
A skipped start codon
A skipped exon
A skipped intron
Which initiation factor mediates the transfer of the initiation complex to the 5' cap of mRNA?
EF-2
EF-1
EF-4A
EF-4E
Which protein recognizes tRNA and its anticodon to transfer it to the A site, and also possesses GTPase activity??
eF-1
eF-2
eEF-1
eRF-1
Which protein serves as the eukaryotic translocase?
eEF-2
eEF-1
eIF-2
EF-1
How are eRF-1 and eRF-3 able to recognize stop codons?
Proofreading mechanisms
Mimic tRNA structure
They don't.
Another protein is responsible (eRF-3)
What % variation is generally accepted for a gene to be considered polymorphic?
1
2
5
10
In a synonymous mutation, there is
an amino acid change
no amino acid change
a missense mutation
a silent mutation
What are the possible results of a non-synonymous mutation?
Missense mutation
Nonsense mutation
Silent mutation
Frameshift mutation
What is the most extensively studied CYP with regards to SNP mutations?
3A4
2D6
1A1
2D9
An extensive metabolizer has
higher than average metabolism
lower than average metabolism
normal metabolism
absent metabolism
Which of these would cause an individual to be considered an ultra-rapid metabolizer?
Duplication
Deletion
Mutation
Missense
A poor metabolizer has
decreased metabolism
increased metabolism
normal metabolism
no metabolism
Which enzyme will metabolize 6-mecaptopurine into a toxic metabolite?
TPMT
HPRT
GAMT
UGT
Which enzyme will metabolize 6-mecaptopurine into a non-toxic metabolite?
TPMT
HPRT
GAMT
UGT
Which enzyme converts irinotecan into SN-38?
CES
UGT
TPMT
HPRT
Which family of enzymes converts SN-38 to SN-38G?
UGT
CES
1A*
3A*
How does mRNA know where to go?
zip code
postal code
pass code
pass word
Where in mRNA is the code contained for localization?
3' UTR
Poly-A tail
5' Cap
Exons
What factors decrease protein synthesis rates?
Deprivation of growth factors
Viral infections
Sudden temperature increase
Hypoxia
Under normal conditions, how is eIF-2 activated?
ATP activation via eIF-2B
GTP activation via eIF-2B
ADP activation via eIF-2B
GDP activation via eIF-2B
Under stress conditions, how is eIF-2 inactivated?
Phosphorylation
Guanylation
Hydrolyzation
Lysosome
How is eIF-4E activated?
Dissociation of 4E-BP
Phosphorylation
Dephosphorylation
Dissociation of eIF-4G
How is eIF-4E inactivated?
Phosphorylation
Dephosphorylation
Dissociation of eIF-4G
mTOR
What is mTOR's role?
Phosphorylating 4E-BP
Phosphorylating eIF-4E
Phosphorylating eIF-2B
Phosphorylating eIF-2A
Which initiation factor binds to the 5' cap of mRNA?
eIF-4E
eIF-4G
eIF-2B
4E-BP
What is IRES?
Internal Revenue Entry Service
Internal Ribosomal Entry Site
Internal Ribosomal Exit Site
Internal Revenue Exit Service
During iron starvation, ferritin ________ while transferrin ______.
decreases, increases
decreases, decreases
increases, decreases
increases, increases
During iron excess, ferritin ________ while transferrin ________.
decreases, increases
increases, decreases
decreases, decreases
increases, increases
What are the domains of the Signal Recognition Particle (SRP)?
GTP-ase/SRP receptor
Translational pause
Signal sequence pocket
DNA binding
What is HSP70's function?
facilitate correct folding
incorrectly folded -> correctly folded
chaperone to lysosome to degrade
literally nothing
What is HSP60's function
facilitate correct folding
misfolded -> correctly folded
lysosomal degradation
literally nothing
What is HSP90's function
phosphorylation
acetylation
nitrosylation
sulfation
What is the 19S cap of the proteasome responsible for?
recognition and unfolding
digestion
preventing protein loss
increase ER chaperone expression
What is the 20S cylinder of the proteasome responsible for?
recognition and unfolding
digestion
ER chaperone expression
ER stress
Where is the proteasome NOT located?
cytosol
ER lumen
Which class of enzymes are responsible for phosphorylation?
Phosphorylases
Protein kinases
Carboxylases
Sulfases
What pathway utilizes hexokinase, and what energy source does hexokinase use?
Glycolysis, ATP
Glycolysis, GTP
Gluconeogenesis, ATP
Gluconeogenesis, GTP
What cell process are CDKs involved in?
Cell cycle
Cell apoptosis
Cell metabolism
Cell 2nd messenger
What steps must be taken to activate CDKs?
Phosphorylation
Dephosphorylation
Cyclin binding
cAMP binding
How does GTP cause activation?
Transferring phosphate
Conformational change
Competitively bind
Remove phosphate
How does ATP cause activation?
Competitively bind
Transfer phosphate
Conformational change
Remove phosphate
Which proteins exchange GDP for GTP to turn on a signal?
GEFs
GUFs
GRFs
GPFs
Which proteins terminate signaling via GTP hydrolyzation?
GAPs
GEFs
CDKs
PDKs
What function does acetylation bring?
Loosens histone binding
Loosens misfolded proteins
Flags DNA for proofreading
Flags proteins for proteolysis
Euchromatin is
less condensed than heterochromatin, transcriptionally active
more condensed than heterochromatin, transcriptionally active
less condensed than heterochromatin, transcriptionally inactive
more condensed than heterochromatin, transcriptionally inactive
Heterochromatin is
more condensed than euchromatin, transcriptionally inactive
more condensed than euchromatin, transcriptionally active
less condensed than euchromatin, transcriptionally active
less condensed than euchromatin, transcriptionally inactive
The ubiquitination enzyme E1 causes
thioester linkages
conjugation
ligation
The ubiquinitation enzyme E2 causes
thioester linkage
coupling
ligation
The ubiquitination enzyme E3 causes
thioester linkages
coupling
ligation
In which organelle(s) does glycosylation occur?
ER
Golgi
Nucleus
Mitochondria
To which amino acid residues does N-linked glycosylation occur?
Asparagine
Arginine
Alanine
Methionine
To which amino acid residues does O-linked glycosylation occur?
Asparagine
Threonine
Serine
Arginine
A protein with the signal 'KDEL' will be
Imported into the nucleus
Exported out of the nucleus
Retained in the ER lumen
Exported out of the cell
A protein with the signal 'KKKKRK' will be
Retained in the ER Lumen
Imported into the nucleus
Exported out of the nucleus
Exported out of the cell
A protein with an abundance of hydrophobic leucine residues will be
Retained in the ER Lumen
Imported into the nucleus
Exported out of the nucleus
Exported out of the cell
What is/are the main region(s) of the golgi apparatus?
Cis
Stacks
Trans
What enzymes do statins target to inhibit cholesterol synthesis?
HMG Reductase
HMG-CoA Reductase
CoA Reductase
LDL-R density
How does Ezitimibe lower serum LDL levels?
Increase LDL-R density
Decrease LDL-R density
Competitively bind to LDL-R
Sequester LDL
How does the pH of the lysosome act as a safety factor?
Lysosomal enzymes can't function in higher pH
Lysosomal enzymes can't function in lower pH
This is a trick, pH has no effect
Lysosomal enzymes use acidic pH to break down proteins
What mechanism does POMC undergo?
Regulated pathway
Lysosomal degradation
Vesicular budding
Ubiquitination
Activation of an ionotropic receptor causes
Ion flux
Ligand entry
cAMP signaling
CDK activation
At the neuronal synapse, the influx of calcium on the presynaptic neuron causes
neurotransmitter release
hyperpolarization of postsynaptic neuron
depolarization of postsynaptic neuron
cancellation of neuronal signaling
An excitatory signal would cause the postsynaptic neuron to open
sodium channels
chloride channels
calcium channels
potassium channels
An inhibitory signal would cause the postsynaptic neuron to open
sodium channels
chloride channels
calcium channels
potassium channels
How many transmembrane domains does a GPCR have?
3
5
7
9
The end result of GPCR activation is
ion flux
cAMP signaling
ligand entry
CDK activation
Which subunit of a GPCR will interact with adenylyl cyclase?
α
β
γ
δ
G protein targets include
cAMP
IP3
Ca2+
Ion channels
When comparing Receptor Tyrosine Kinases, the largest variation occurs on the
intracellular domain
extracellular domain
transmembrane domain
How does a ligand activate an RTK?
dimerization
monomerization
ion flux
g-protein signaling
How is the cell able to terminate receptor activity?
degradation of agonist
receptor uncoupling
receptor endocytosis
receptor down-regulation
How does steroid binding affect DNA?
exposure of binding site
HSP90 release
HSP90 recruitment
concealment of binding site
What is the late response/secondary response for steroid hormones?
primary response products cause deactivation
secondary response products cause deactivation
primary response products cause amplification
secondary response products cause amplification
______ and ______ help prevent mRNA degradation by forming a circular complex with mRNA
eIF-4A
eIF-4G
eIF-2
eIF-4E
