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cell bio exam 3

front 1

top 3 leading cancer related deaths

result from proto-oncogene activation and TSG inactivation

back 1

lung

breast/prostate

colorectal

front 2

minimum amount of DNA alterations needed for a cell to become malignant

back 2

6

front 3

process of a normal cell evolving into a highly malignant cell

back 3

tumor progression

front 4

transcription factor, most frequently mutated gene in cancer, guardian of the genome, regulates at G1- growth arrest and apoptosis, suffers from point mutation which inactivates it -resulting in no DNA repair

back 4

p53

inactivated in 50% of all cancers

front 5

genes that are like the car brakes, help regulate cell growth, gives loss of function to mutant genes

back 5

TSG

tumor suppressor genes

front 6

cell dividing out of control, mutant form of normal has genes, dominant genes, code for RTK, G proteins, transcription factors, Ras gene, classified as

back 6

oncogene

front 7

normal cell division like a gas pedal on a car, but has the potential for a gain-of-function in cancer, these genes are

back 7

proto-oncogene

front 8

signaling that effects the same cell

back 8

autocrine

front 9

signaling that effects neighboring cells, even of a different type

back 9

paracrine

front 10

long distance signaling that is able to signal the whole body, usually through the circulatory

back 10

endocrine

front 11

high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones, key regulators of normal cellular processes but also to have a critical role in the development and progression of many types of cancer

back 11

enzyme-coupled receptors

Receptor tyrosine kinases (RTK)

front 12

how does the G-protein coupled receptor work

back 12

Binding of an agonist results in a conformation change in the receptor that is transmitted to the bound α subunit, the α subunit exchanges GTP in place of GDP which in turn triggers the dissociation of it from the βγ dimer and from the receptor. The dissociated α subunit interacts with other intracellular proteins to continue the signal transduction cascade

front 13

a large protein family of receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. They are called seven-transmembrane receptors because they pass through the cell membrane seven times, ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. They are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs

back 13

G-protein coupled receptor

guanine nucleotide

front 14

general name for a group of more that 100 diseases in which cells in a part of the body begin to grow out of control

back 14

cancer

front 15

Conversion of an impulse or stimulus from one physical or chemical form to another. In cell biology, the process by which a cell responds to an extracellular signal.

back 15

signal transduction

front 16

Protein that recognizes and responds to a specific signal molecule.

back 16

receptor

front 17

A set of proteins and small-molecule second messengers that interact with each other to relay a signal from the cell membrane to its final destination in the cytoplasm or nucleus.

back 17

intracellular signaling pathway

front 18

Extracellular signal molecule that is secreted and transported via the bloodstream (in animals) or the sap (in plants) to target tissues on which it exerts a specific effect.

back 18

hormone

front 19

The molecular mechanisms by which cells detect and respond to external stimuli and send messages to other cells.

back 19

cell signalling

front 20

what do vSNARES do

back 20

SNAREs on the vesicle compliment the target tSNAREs

front 21

in order to use protein translocators, is the protein folded or unfolded?

how about a nuclear pore?

back 21

unfolded to go through the membrane

folded to go through the nucleus

front 22

Which of the following is true of lysosomes?

A. The products of digestion in lysosomes leave the lysosome by transport vesicles.
B. Most of the lysosomal membrane proteins have glycosylated regions on the cytosolic side of the membrane.
C. Lysosomal enzymes are optimally active in the acidic conditions maintained within lysosomes.
D. Lysosomes form from vesicles that pinch off from the endoplasmic reticulum

back 22

c

front 23

Proteins destined for regulated secretion:

A. have special surface properties that cause them to form aggregates that are packaged into secretory vesicles.
B. have a series of amino acids that act as a tag that marks them for packaging into secretory vesicles.
C. are cleaved from membrane domains in the Golgi apparatus prior to being packed into secretory vesicles.

back 23

a

front 24

Which type of protein binds to improperly folded or improperly assembled proteins in the ER, holding them there until proper folding occurs?

A. Tethering proteins
B. Glycosylating proteins
C. Chaperone proteins
D. Antibody proteins

back 24

c

front 25

Vesicle budding is driven by the assembly of a protein coat.

A. True
B. False

back 25

a

front 26

The ER signal sequence on a growing polypeptide chain is recognized by a signal recognition particle (SRP) in the cytosol. This interaction:

A. causes the polypeptide chain to dissociate from the ribosome.
B. causes the ribosome to return to the pool of free ribosomes in the cytosol.
C. guides the ribosome and its polypeptide to the ER membrane.
D. speeds the synthesis of the polypeptide chain

back 26

c

front 27

Which of the following is true?

A. A special class of ribosomes embedded in the ER translates the proteins destined for that organelle.
B. A common pool of ribosomes is used to synthesize both the proteins that stay in the cytosol and those that are destined for the ER.
C. All ribosomes are attached to the ER when they are synthesizing a protein.

back 27

b

front 28

Which of the following statements is NOT true of mitochondrial proteins that are synthesized in the cytosol?

A. The proteins are unfolded as they are transported into the mitochondria.
B. The proteins cross both the inner and outer mitochondrial membranes as they are imported.
C. The proteins are transported across the mitochondrial membranes while being synthesized.
D. Chaperone proteins help draw the proteins inside the mitochondrion.
E. The proteins usually have a signal sequence at their N-terminus.

back 28

c

front 29

Which proteins bind to nuclear localization signals on newly synthesized proteins?

A. Nuclear pore proteins
B. Nuclear transport receptors
C. Signal-recognition particles

back 29

b

front 30

The interiors of the ER, Golgi apparatus, endosomes, and lysosomes communicate with each other in which of the following ways?

A. By small vesicles that bud off of one organelle and fuse with another
B. By open pores that allow ions to exit and enter the organelles
C. They do not communicate with one another.
D. By excreting hormones and other small signaling molecules

back 30

a

front 31

Which organelle is essentially a small sac of digestive enzymes that functions in degrading worn-out organelles, as well as macromolecules and particles taken into the cell by endocytosis?

A. An endosome
B. The Golgi apparatus
C. A lysosome
D. The endoplasmic reticulum
E. A peroxisome

back 31

c

front 32

Which organelle sorts ingested molecules and recycles some of them back to the plasma membrane?

A. An endosome
B. The Golgi apparatus
C. A lysosome
D. The endoplasmic reticulum
E. A peroxisome

back 32

a

front 33

Which organelle receives proteins and lipids from the endoplasmic reticulum, modifies them, and then dispatches them to other destinations in the cell?

A. A mitochondrion
B. An endosome
C. The Golgi apparatus
D. The nucleus
E. A peroxisome

back 33

c

front 34

what signals for proteins to have parts of them embedded in the membrane ER

back 34

stop transfer sequence

start transfer sequence

both hydrophobic

front 35

two protein components help guide ER signal sequences to the ER membrane

back 35

signal recognition particle (SRP) in the cytosol binds with the ribosome and the signal sequence

SRP receptor embedded in the ER membrane recognizes the SRP

front 36

2 kinds of proteins transferred from the cytosol to the ER

back 36

water soluble completely translocated

prospective transmembrane partly translocated ( embedded in membrane )

front 37

small membrane enclosed organelles that contain several enzymes that produce hydrogen peroxide and have a variety of other functions, derived from the endoplasmic reticulum or replicate by fission- it also transports proteins via translocation

back 37

peroxisome

front 38

main site of lipid synthesis

back 38

ER

front 39

how do proteins know to go to the mitochondria

back 39

signal sequence at their N-terminus recognized by a chaperone protein that grabs it, unfolds it, the folds back once entered, requires ATP

use a translocator channel- similar to a nuclear pore, but instead of one big pore, it is one in each bi-layer

front 40

how are mitochondria and chloroplasts similar to nucleus

back 40

double phospholipid bi-layer

own DNA and therefore own proteins

recognize signal sequence- positive charge hydrophobic AA

front 41

what brings proteins to the nucleus

back 41

importin- nuclear import receptors

take the protein in its 3 prime shape unlike other oraganelles

front 42

how do proteins get to where they need to go

back 42

signal sequence- nuclear localization signal

positive charged hydrophobic lysine and arginine

binds to the nuclear import receptor to bring it in - requires GTP for energy

front 43

nuclear pores are made of

back 43

30 proteins complex, act as a gate for proteins to enter and RNA to exit

front 44

inner nuclear membrane conatins

back 44

membrane most similar to the cell membrane and is continuous with the membrane of the ER

front 45

inner layer of nuclear membrane conatins

back 45

proteins and binding sites for chromosomes

nuclear lamina for structural support

front 46

how many membranes of the nuclear envelope, aka nuclear membrane

back 46

4

double phospholipid bi-layer

inner and outer

front 47

The lac operon:
A. is found in eukaryotic cells
B. codes for the sequence of amino acids in lactase
C. regulates translation of mRNA
D. regulates transcription by turning on or off the production of a repressor protein
E. regulates DNA replication by turning on or off the production of an inducer protein

back 47

d

front 48

At the E site

A)transfer RNA is released

B)anticodons match with codons

C)peptide bonds are formed between amino acids

D)transcription occurs

back 48

a

front 49

An activator must react with its substrate before it can bind to DNA.

A)True

B)False

back 49

a

front 50

Negative control occurs when a repressor is inactivated by an inducer.

A )True

B)False

back 50

a

front 51

In regulation by induction

A)an inducer inactivates the repressor so transcription can proceed

B)an inducer inactivates the repressor so transcription is stopped

C)an inducer activates the repressor so transcription can proceed

D)an inducer activates the repressor so transcription is stopped

back 51

a

front 52

In regulation by repression

A)a sugar, such as lactose, acts as an inducer and combines with the repressor to prevent transcription

B)an inducer activates the activator so that it binds to DNA and prevents transcription

C)an amino acid activates the repressor so that the repressor binds to the operator and prevents transcription

D)an amino acid binds to the operator, blocking the repressor, allowing transcription to proceed

back 52

c

front 53

Transcription is turned off by

A)induction

B)repression

C)activation

D)all of the above

back 53

d

front 54

how does the cell know what proteins go where

back 54

1. signal patches made of amino acid residues that are distant to one another in primary form but are close together in tertiary structure

2. sorting signal made of amino acid sequences

no signal= stays in cytosol and functions there

front 55

proteins transported to the nucleus are completely synthesized in the cytosol and ______ before import, unlike other organelles

back 55

correctly folded

front 56

three ways proteins are transported throughout the cell

back 56

1. through nuclear pores from cytosol into nucleus

2. across organelle membranes via protein translocators

3. by transport vesicles through plasma membrane to outside of cell

front 57

two ways cells can isolate and organize their chemical reactions

back 57

aggregate different enzymes

confine different metabolic processes within different membrane enclosed compartments (organelles)

front 58

large protein complexes found in the cytosol and nucleus that have protease activity

back 58

proteosomes

front 59

enzymes that degrade proteins by a process known as proteolysis (hydrolyzes peptide bonds)

back 59

proteases

front 60

regulatory RNA's work by

back 60

base pairing with complementary sequences within target mRNA's, leading to mRNA degradation and inhibition of translation

front 61

two key aspects of eukaryotic translation are regulated by phosphorylation- same as effects in DNA transcription

back 61

1. recognition of the mRNA by ribosome can be inhibited by PO4

2. 5' cap binding proteins can be bound by non-PO4 binding proteins

front 62

proteins that block the translation of mRNA because they prevent the attachment of ribosomes by binding to specific nucleotide sequences in the 5' untranslated region (promoter)

back 62

translation repressor

front 63

translation of mRNA is regulated by regulatory proteins that are needed so ribosomes can translate mRNA are called

back 63

translation factors

front 64

three chemical modifications to histones to regulate transcription

back 64

1.activator- histone acetyltransferases (nucleosomes loosened)

2.repressor- histone deacetylases

3.repressor- histone methyltransferases

front 65

two ways transcription regulators act

back 65

1.directly effect the assembly process that require RNA polymerase and transcription factors at the promoter- histone proteins

2.modify the chromatin structure of promoter regions- DNA itself

front 66

cell defense mechanism that destroys foreign RNA, man made, double stranded

back 66

siRNA

front 67

controls gene expression, single stranded, regulate our own genes, base pairs with specific mRNA

back 67

miRNA

front 68

in the absence of lactose, the lac repressor

A)binds to the operator and prevents transcription

B)binds to the CAP site and prevents transcription

C)binds to the CAP site and facilitates transcription

D)binds to the operator and facilitates transcription

back 68

a

front 69

The main regulatory gene that acts on the lac operon is a

back 69

lac repressor with no lactose and CAP activator with no glucose

repressor binds to the lac operon operator, where it blocks RNA polymerase from transcribing the lac operon

CAP binds to cyclic cAMP before it can bind to DNA, switches on genes to increase intracellular cAMP

front 70

In a eukaryote, activating transcription factors may stimulate gene expression by binding to a DNA site called a(n) _____.

back 70

enhancers

front 71

You have inserted the gene for human growth factor into the E. coli lactose operon, replacing the structural genes with the gene for human growth factor. What substance must you add to your culture of bacteria to cause them to produce human growth factor for you?

back 71

allolactose

front 72

In an inducible operon, the inducer is often the _____ in the pathway being regulated; the inducer binds to the _____, thus rendering it _____.

back 72

substrate ... repressor ... inactive

front 73

the genetic information contained within the order of nucleotides in mRNA is interpreted to generate the linear sequence of amino acids

back 73

translation

front 74

which part of the mRNA is used

back 74

middle

front 75

the protein coding region with nonoverlapping string of codons

back 75

ORF- open reading frame

front 76

translation starts at what end

back 76

5' to the 3'

front 77

how many possible codons

back 77

3 bases, 4 nucleotides = 43 = 64

61 are translated into AA, the rest are stop codons

front 78

provides the genetic information template to be translated

back 78

mRNA

front 79

provides the interface between the mRNA and their corresponding AA

back 79

tRNA

front 80

enzyme links AA to their corresponding tRNA, one for each of the 20 AA

back 80

aminoacyl-tRNA synthetase

front 81

coordinates recognition between the mRNA and corresponding tRNA and catalyzes the peptide bond formation between tRNA associated AA

back 81

ribosomes

front 82

does transcription and translation occur at the same time in eukaryotes

back 82

no

one is in the nucleus and the other in the cytoplasm

front 83

three binding sites in the ribosome

back 83

A- enters

P- attaches AA

E- exit

front 84

what determines the start of translation

back 84

5' end of ORF is methionine (AUG)

front 85

base pairing results in structural conformational change which in turn causes some of the bound initiation factors to be

back 85

released and new ones bind

front 86

in addition to codon-anticodon base pairing, the ribosome has additional proofreading mechanisms to ensure

back 86

the correct tRNA is brought into the A site

front 87

stop codons are recognized by proteins called

back 87

release factors

activates hydrolysis of the polypeptide from the tRNA

front 88

an mRNA with multiple ribosomes attached is a

back 88

polyribosome

front 89

Which type of RNA includes the anticodon and brings the amino acids to the site of protein synthesis?

a. mRNA
b. rRNA
c. tRNA
d. DNA
e. mDNA

back 89

c

front 90

Where does translation occur?

A.Cytoplasm

B.Nucleus

C.Mitochondria

D. Ribosome

back 90

a

front 91

Which molecule contains codons?

A)DNA

B)mRNA

C)tRNA

D)rRNA

back 91

b

front 92

What form of RNA binds to both the codon and an amino acid?

A)mRNA

B)tRNA

C)rRNA

D)None of the above.

back 92

b

front 93

What area of a gene does the RNA polymerase bind to?

A)promoter

B)exon

C)intron

D)codon

back 93

a

front 94

RNA is transcribed using the ____ strand of DNA.

A)coding

B)alternate

C)template

D)non-template

back 94

a

front 95

Which of the statements below is FALSE?

A)The genetic code is overlapping.

B)The genetic code is universal.

C)Degenerate codons specify the same amino acids

D)The genetic code is triplet in nature.

back 95

a

front 96

The first mRNA codon to specify an amino acid in a protein sequence is always _____.

A)TAC

B)UAA

C)UAG

D)AUG

back 96

d

front 97

Transfer RNAs bind to messenger RNAs during translation via their _____.

A)codon

B)anticodon

C)template

back 97

b

front 98

Of the ____ different possible codons, ____ specify amino acids and ____ signal stop.

A)20; 17; 3

B)180; 20; 60

C)64; 61; 3

D)61; 60; 1

back 98

c

front 99

An antibiotic interferes with the ability of the ribosome to move. What effect would exposure to this chemical have on a bacterial cell?

A)Protein synthesis will be enhanced.

B)The protein synthesized will be shorter than normal.

C)The protein synthesized will be longer than normal.

D)No proteins will be produced.

back 99

d

front 100

What sequence on the template strand of DNA corresponds to the first amino acid inserted into a protein?

A)TAC

B)UAA

C)UAG

D)AUG

back 100

a

front 101

Which of the following is an example of the degeneracy of the genetic code?

A)A given amino acid has more than one codon.

B)Each codon specifies more than one amino acid.

C)The first base specifies the amino acid.

D)The genetic code is not degenerate

back 101

a

front 102

During translation, the _____ site within the ribosome holds the growing amino acid chain while the ____ site holds the next amino acid to be added to the chain.

A)A; P

B)P; A

C)A; B

D)B; A

back 102

b

front 103

Translation terminates when _____.

A)the A site is empty

B)a stop codon is present in the A site

C)a release factor is present in the P site

D)translation reaches the end of the mRNA

back 103

b

front 104

what dictates which genes are expressed, where, and when

back 104

regulatory mechanisms

front 105

we rarely use any more of _____ % of our genes at any given time

back 105

5-10%

front 106

all cells have the same DNA and therefore the same

back 106

genes

but they are not all expressed- gives specificity to muscle, nerve, skeletal cells

front 107

all cells require

back 107

ATP

front 108

what events does gene expression control

back 108

when and how often a gene is transcribed

how mRNA is spliced

which mRNA is transported

how quickly mRNA is degraded

which mRNA is translated

how quickly protein is degraded

front 109

what stage is the most regulated

back 109

initiation of transcription

front 110

slight continuous level of expression of a gene

back 110

basal level

front 111

transcription activator proteins bind to the DNA and RNA polymerase near the promoter which brings in the RNA polymerase to the promoter

back 111

cooperative binding resulting from recruitment

an indirect mechanism because of the domino effect

front 112

two proteins acting in one complex, need both of them to be active, one end binds to the DNA binding site, the other end binds to the RNA polymerase

back 112

dimer

front 113

set of three genes plus other things in E. coli involved in the transport and breakdown of lactose into glucose

back 113

lac operon

front 114

what is the lac operon composed of

back 114

3 genes- lacZ, lacY, lacA

promoter

terminator

operator

front 115

what is the lac operon regulated by

back 115

availability of lactose and glucose

front 116

how does a cell use lactose as energy

back 116

produces beta-galactosidase to break down lactose into glucose

front 117

lac promoter directs transcription of all 3 genes as a single mRNA molecule called

back 117

polycistronic message

front 118

what does lacZ do

back 118

produces enzyme beta-galactosidase to break down lactose into galactose and glucose

front 119

what does lacY do

back 119

produces the protein lactose permease that transports lactose into the cell

front 120

what does lacA do

back 120

produces the enzyme thiogalactosidase transacetylase to break down the toxic thiogalactosidase that was brought into the cell with lactose

front 121

when lactose is present and glucose is not then the genes are

back 121

expressed

front 122

regulation in the expression of the lac operon is upstream and controlled by

back 122

if or not there is an activator

CAP

lac repressor which is encoded by a gene

front 123

gene that encodes the lac repressor that binds to the lac promoter region and prevents transcription when there is no lactose

back 123

lacI gene and allolactose

front 124

when glucose is present but there is no lactose, then

A)cyclic AMP is high, the catabolite activator protein (CAP) binds to the activator binding site, and transcription of lactose is turned on

B)cyclic AMP is low, CAP binds to the site activator binding site, and transcription of lactose is turned on

C)cyclic AMP is high, CAP does not bind to the activator binding site, and transcription of lactose is turned on

D)cyclic AMP is low, CAP does not bind to the activator binding site, and transcription is turned off

back 124

d

inhibitor activated

lac repressor binds to operator region and prevents RNA polymerase from binding

front 125

when glucose is absent but lactose is present, then

back 125

promoter activated

an allosteric effect on CAP binding site

cyclic cAMP binds to CAP which then binds to the CAP site on mRNA and RNA polymerase then attaches to the promoter site so transcription can occur

front 126

when both glucose and lactose are present

A)cyclic AMP is high so transcription occurs

B)the lac repressor binds with the lactose and transcription occurs

C)RNA polymerase is able to bind to the operator so transcription occurs

D)transcription is at a minimal level

back 126

d

a basal level of transcription occurs

front 127

protein exerts its effects from a distance away from the promoter region

works by changing the structure of the mRNA so it bends around in a loop,

can activate or repress

back 127

enhancer site for binding of an activator protein