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Biology 203 > Exam 2 > Flashcards

Exam 2 Flashcards

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1
Q

Ciliary Biogenesis From Basal Bodies

A

Basal body pair located beneath plasma membrane, Basal body begins to elongate and push the membrane outwards

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2
Q

Ciliopathies

A

Immotile cilia syndrome
Hydrocephalus – wet brain disease
Retinitis pigmentosa – Degeneration of retina, causes blindness
Polycystic kidney disease
Situs inversus – reversal in internal organs
Bardet-Biedl syndrome – Blindness & Loss of Smell

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3
Q

Motile Cilia Locations

A

Central Nervous system, Respiratory tract, Fallopian tubes, Sperm

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4
Q

Primary Cilia

A

All cells in the human body have at least one, non motile, >= one per cell, used to sense the surrounding environment

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5
Q

Flagellum

A

Threadlike structure used to move single cells (Sperm, protazoa)

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6
Q

Stroke pattern in motile Cilia

A

Breast stroke pull, effective stroke, recovery, repeat

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7
Q

Stroke pattern in motile flagella

A

undulation pattern

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8
Q

Anatomy of a Motile Cilium

A
  • Encased in a cell membrane
  • Central unfused pair of microtubules
  • surrounded in fused pairs of microtubules connected by Dynein proteins
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9
Q

Intra-Ciliary Transport Components

A

Cilia grow at the tip using transport proteins to bring material from the centrosome. Uses Dynein and Kinesin like MT.

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10
Q

Doublet Microtubule Sliding

A

When ATP is added, outer doublet slide past one another toward the + end

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11
Q

Immotile Cilia Syndrome

A

Caused by genetic mutations, lead to infertility and many other cilia disorders

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12
Q

Cause of Immotile Cilia Syndrome

A

Abnormal flagellum, Axoneme is normal except for the absence of the Dynein arms

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13
Q

Hydrocephalus

A

Caused by immotile cilia, not circulating fluid within brain ventricles, infant enlarged brain, can cause mental retardation

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14
Q

Retinitis Pigmentosa

A

Degenerative genetic disease, eventually leads to blindness, Kinesin mutation and no rhodopsin transport along microtubules in retinal cells

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15
Q

Situs Inversus

A

Causes some of the bodily organs to be flipped

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16
Q

Microtubule Structure

A
  • Walls made up of protofilaments, appear as beaded strings
  • Cross section shows a central lumen
  • 13 Protofilaments form the tube shape
  • Stretch from the Microtubule Organization Center (negative end same end as MTOC)
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17
Q

Role of Y-tubulin

A

aids the alpha and beta molecules that make up the tubule, y tubulin allows for the alpha and beta to form a conical structure which serves as a model for the alpha and beta molecules to form the structure of the microtubule

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18
Q

Dynamic Instability Experiment

A 
Experiment
-Depolymerize the current microtubules
-Repolymerize from the MTOC
-Inject fluorescent tubulin
Observe:
-Slowly grow out from the MTOC
-Rapidly shorten at times but do not disappear
-Repeat
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19
Q

Building and breaking down microtubules

A

GTP-tubulin cap at the + end, primer for addition of more subunits, more GTP-tubulin adds to the cap, GTP slowly turns into GDP, if GTP in the cell is low the GTP will be hydrolyzed to GDP which forms an unstable cap that begins to break apart

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20
Q

MT Depolymerization

A

Colchicine used to depolymerize then test the process again to see impact of MT

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21
Q

MT stabilization

A

Taxol used to prevent MT depolymerization, used as chemotherapy drug

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22
Q

Cell Shape Microtubule Experiment

A

Colchicine depolymerizes MT, cell changes shape, re-stabilize with taxol and the cell returns to original shape

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23
Q

Dynein Motor Protein

A

Retrograde, moves toward the MTOC

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24
Q

Kinesin Motor Protein

A

Anterograde, moves away from the MTOC

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25
Cytosolic Ribosomes
Where all cellular proteins begin their synthesis
26
Constitutive Secretory Vesicle
Once the molecule gets in the vesicles, it continues pumping out of the cell continuously
27
Regulative Secretory Vesicle
Material gets in the vesicles and then remains in the cell until there is an order telling it to go to the membrane ( Digestive enzymes, peptide hormones )
28
Endoplasmic Reticulum Structure
Bilayer sheet, allows for rapid increase in surface area, will begin to fold once large enough
29
Functions of Smooth Endoplasmic Reticulum
Enzymatic pathway for synthesis of: Membrane phospholipids, cholesterol, fatty acids, DOES NOT HAVE RIBOSOMES
30
Flippase
Flips synthesized molecule so that it will fit in the structure of the bilayer
31
Phospholipid synthesis in the smooth ER
Everything made while facing cytosol, flippase allows for the molecules to take part in the bilayer
32
Protein Targeting of ER
Proteins destined for secretory pathways will bind to the ER, then become encapsulated to move throughout the cell or to the Golgi for secretion
33
General Protein Rule
All synthesized proteins on the bound ribosomes will be secreted from the cell unless there is a counteracting order
34
Protein Targeting Steps
1. Signal sequence to find free ribosomes 2. Signal Recognition Particle binds the free ribosomes 3. SRP receptor contains recognition site, binds to ER and releases SRP allowing protein synthesis to resume on the ribosome 4. Signal Sequence Receptor binds, allowing the ribosome to bind to ER membrane channel 5.
35
Initiation of Glycoprotein Synthesis in the Rough ER
Growing protein enters the ER lumen, pre made oligosaccharide transferred to amino acid on growing peptide chain
36
Heat Shock Gene
Certain genes undergo greatly increased transcription under elevated temperatures (Enlarged bands called puffs)
37
Molecular Chaperone Action
Newly made proteins become associated with a chaperone protein, chaperone bends the protein to shape, ATP causes the chaperone to straighten out and release the folded protein
38
Unfolded Protein Response
Protein enters ER via transport, proteins that are incorrectly folded will bind to ER receptors to produce a transcription regulator, misfolded proteins are degraded by proteasome pathway
39
Origin of the Endoplasmic Reticulum
Eukaryotes have the ER to accomplish the same tasks that bacteria use their Plasma membranes for, so the ER likely came from the plasma membrane
40
Aspects of Normal Protein Folding
Proteins must be folded correctly to gain function, assisted by chaperone proteins, non-covalent forces interact
41
Causes of Protein Misfolding
pH changes, temperature changes, toxic chemicals, genetic causes
42
Protein Misrouting (Pathogenicity)
Misfolding causes cell to tag protein, proteins will be unable to go to their intended locations, functional protein is destroyed by proteasomes
43
Cause of Alzheimers
Development of plaques of protein in spaces between neurons and the protein
44
Parkinson's Disease
Decrease of neural secreted dopamine, clumps of proteins located in brain cells causing them to break down and die
45
Bacteria Vs Eukaryotes
Nuclear envelope presents an additional opportunity for controlling gene expression, given that all proteins are made in the cytosol
46
Significance of Nuclear Envelope
Elaboration of the ER, separates mRNA transcription site from cytoplasmic ribosomes where translation occurs
47
Significance of Nuclear Pore Complex
Arose from the need to cross the membrane barrier, 60,000 protein molecules per minute, can serve to keep transcription factors from gene targets
48
Nuclear Lamina
fibrillar network inside the nucleus, regulates important cellular events such as DNA replication and cell division, anchors the nuclear pore complexes embedded in the nuclear envelope
49
Nuclear Lamina Structure
envelope cytoskeleton, intermediate filament class, binding sites for membrane and chromosomes, structural integrity to nucleus
50
Nuclear Pore Structure
octagonal symmetry, passes through both nuclear membranes, cytoplasmic and nuclear ring,
51
Nuclear Pore Function
transport of molecules across the nuclear envelope, ncludes RNA and ribosomal proteins moving from nucleus to the cytoplasm and proteins (such as DNA polymerase and lamins), carbohydrates, signaling molecules and lipids moving into the nucleus
52
Nuclear Envelope during the cell cycle
Present during interphase, vanishes during mitosis, reappears at telophase
53
Nucleocytoplasmic Transport
1. Nuclear Localization Signal binds to cargo protein 2. NLS Receptor (importin) binds to the NLS 3. B protein bonds to the a-importin 4. B protein interacts with the cytosoloic ring of the Nuclear Pore 5. Entire material imported into the nucleus 6. a and b proteins are recycles into the cytoplasm
54
Nuclear signal fusion
Nuclear localization signal is added into a non-nuclear protein, that protein is then found in the nucleus later
55
Nucleolus in the Cell Cycle
Present during interphase, vanishes during mitosis, two nucleoli per cell, reappears at telophase
56
Fibrillar Center
Location of DNA
57
Dense Fibrillar Center
Site of newly transcribed pre-rRNA, site of some pre-rRNA processing steps
58
Granular Component
Site for ribosomal subunits storage
59
Pulse Chase Autoradiography experiment
Hypothesis: RNA synthesis occurs in the DFC Experiment: Pulse-Chase 1. Expose cell to radioactive uridine to be absorbed by new RNA 2. 'Chase' - wash away the Uridine 3. Place a layer of film over the material to create an image Conclusion: Genes that code for something are located in the DFC, and genes that dont are located in the FC region
60
Autoradiograph
Layer of film placed over material previously exposed to radiation
61
Nucleolar Organizer Locus
Visible band located on some metaphase chromosomes, identical to the FC region of the nucleus, site of RNA polymerase I
62
Gene Position Experiment
Hypothesis: RNA genes are located in the NOR region Experiment: In situ hybridization 1. radioactive RNA will pair up with DNA that coded for it 2. Place a layer of film over the chromosome to see where the genes are located 3. Conclude these genes are located in the NOR
63
Nucleolar Cycle
1. Prophase, DFC Disappears 2. Metaphase, Anaphase, GC disappears and FC regions remain 3. Telophase, DFC Reappears 4. Telophase, GC Reappears
64
Nucleolar Biogenesis Experiment
Hypothesis: Prove if one copy of rRNA can code for the rest of the nucleus Experiment: Microinjection of one rRNA gene 1. Isolate one copy of rRNA, build it into a DNA circle 2. Inject DNA circle into the nucleolus 3. Extra nucleolus appears 4. Conclude one copy of rRNA can produce an entire nucleolus
65
3 locations of a ribosome
Cytosol, chloroplasts, mitochondria
66
S subunit factor
depends on the mass and shape of the object, as well as its speed in a centrifuge
67
Start Codon
AUG
68
Structure of Proteins
Amino Acids, Primary Structure (Chain), Secondary Structure (Sheets), Tertiary structure combines multiple secondary structures, Quarternary is final structure

Biology 203 (1 decks)

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