ch 15 Flashcards

(48 cards)

1
Q
A
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2
Q

What is the difference between a Nuclear Localization Sequence (NLS) and a Signal Sequence?

A

NLS sends proteins into the nucleus and uses Ran-GTP to release protein inside nucleus. Protein often folded
Signal Sequence sends proteins into other organelles and uses ATP/GTP, protein often unfolded

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3
Q

T/F: Some signal sequences have more important structural features than specific amino acids sequences

A

True

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4
Q

How does the organelle recognize the signal sequence and allow the protein in?q

A

The organelle has a receptor that recognizes the signal sequence and allows to cross the organelle’s membrane using ATP and a protein channel/transporter

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5
Q

What is the signal sequence for import into ER?

A

2nd longest, look for bunch of Leu.

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6
Q

Signal sequence for retention in lumen of ER?

A

KDEL (Lys-Asp-Glu-Leu) (LAGLEU)

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7
Q

Signal sequence for import into mitochondria

A

N-terminus, very long bunch of Arg

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8
Q

Signal sequence for import into Nucleus

A

Series of Lys (KKK)

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9
Q

Signal for export from nucleus

A

Met - Leu - Leu- Phe (MET DELULU BAE) not all together

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10
Q

Signal sequence for import into peroxisomes

A

Ser-Lys-leu (SKL) South korea L

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11
Q

Which organelle does the nucleus’s outermembrane connect into?

A

the ER

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12
Q

Selective gate that goes through both membranes of the nucleus, allows stuff in and out depending on the molecule, tightly regulated.

A

Nuclear Pore

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13
Q

How do small vs large molecules (proteins) go through nuclear pores

A

Small Molecules: freely diffuse
large molecules: require a Nuclear Localization Signal that is read by nuclear transport receptors to specifically enter nucleus

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14
Q

What is a nuclear localization signal and what is it used for?

A

A short stretch of Lys and Arg that is read by nuclear transport receptors to specifically enter molecule into the nucleus.

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15
Q

Is transport through nuclear pores passive or active?

A

Active, requires energy to move proteins across membrane against gradient

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16
Q

Do proteins remain folded or unfolded when going through nuclear pores?

A

Fully folded

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17
Q

What is Ran?

A

A type of GTPase that regulates the transport of proteins through nuclear pores

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18
Q

RanGTP and RanGDP, which one is inside nucleus and outside? Explain functions of each

A

RanGTP = Inside Nucleus, binds to protein with NLS coming into nucleus, helps release protein inside nucleus
RanGDP = Outside Nucleus, hydrolyzed from GTP to GDP to release proteins outside nucleus

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19
Q

Explain the steps for proteins to enter nucleus through nuclear pores

A
  1. Protein with NLS attaches to Nuclear Transport Receptors in the cytoplasm
  2. Transport Receptor carries protein through nuclear pore into the nucleus
  3. RanGTP binds to transport receptor, causing a conformational change that releases protein inside nucleus
  4. Receptor goes back to cytoplasm
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20
Q

What prevents protein misfolding during transport and helps refold proteins once inside organelle?

A

Chaperonins/Chaperone Proteins

21
Q

Explain how proteins are transported across mitochondrial and chloroplast membranes. use the following vocabulary: N terminal sequence, import receptors, protein trans locator (TOM and TIM) mitochondrial matrix, Chaperonins.

A

Protein binds its N-terminal sequence to import receptors on outer membrane, protein travels through import receptor protein and also goes through protein translocator in outer membrane (TOM) and then the inner one (TIM), protein is unfolded. Once inside mitochondria matrix, signal is cleaved off and protein is refolded with chaperonins.

22
Q

What are the 2 kinds of proteins transferred from cytosol to ER? explain each and what do both have?

A
  1. Soluble Proteins: transferred completely to ER lumen during synthesis, destined to be secreted outside cell or to another organelle (not mitochondria)
  2. Transmembrane Proteins: halfway in ER membrane, destined to reside in ER or membrane of another organelle/plasma membrane

both have a N-termines signal to direct to ER

23
Q

What do proteins need if they want to stay in the lumen of the ER?

A

C terminal signal (KDEL)

24
Q

if a protein does not have an ER signal sequence, where does it gO?

A

it’s synthesized in the cytosol using free ribosomes instead of the ER and will stay there.

25
What are SRPs?
Signal Recognition Particles, are in the cytosol, binds to ER signal sequence on proteins in the middle of synthesis, stop translation. get it because they recognize the ER signal sequence on proteins
26
explain the steps of SRP proteins and what they cause
1. SRP in cytosol binds to ER signal sequence on currently translated protein, stops translation 2. SRP protein complex binds to SRP receptor on rough ER membrane 3. ribosome with currently translated protein is transferred to a translocation channel in the ER membrane, translation resumes and protein is directly synthesized into ER lumen (or ER membrane (transmembrane) 4. Signal peptidase binds to translocation channel until synthesis is done, then cleaves off ER signal sequence 5. protein enters ER, SRP is released and goes back to cytosol
27
What different parts do transmembrane proteins have and multi-pass transmembrane proteins have that cause their orientation in the membrane?
Transmembrane proteins have a hydrophobic stop-transfer sequence , causing the protein to be half in and out of the membrane Multi-pass Transmembrane Proteins have a start and stop-transfer sequence. The start can be in the middle of the protein, which is where the protein will be pushed into the ER. The stop will stop it.
28
Proteins travel through the Golgi’s _____ in ______.
Cisternae, vesicles
29
The golgi decides _____.
where each protein will go next.
30
What is glycosylation? Function/Purpose?
adding a 14-sugar group to the amino acid Asn (asparagine), protects protein from degradation, helps fold correctly, marks for where it should go next
31
What is Disulfide Bond FormatioN?
2 cysteine amino acids connect through a disulfide bond, stabilizes protein structure
32
What prevents unassembled complexes or misfolded proteins from leaving the ER?
chaperonins
33
Misfolded proteins inside the Er activates ______ that causes the _____ gene to be activated.
receptors, chaperone
34
In vesicular Transport, both cargo and destination require ________.
Specificity
35
What are recognition events
when the appropriate organelles has complementary proteins to the ones on the vesicle , allows vesicle to go to right place
36
What part of the vesicle has specific proteins that act as address labels
The vesicles membrane
37
What does clathrin coated vesicles do?
Clathrin is a coat protein that shapes the vesicle into a sphere
38
Dynamin function
protein that pinches off vesicle from membrane
39
What recognizes the specific cargo proteins?
Transport receptors
40
What connects transport receptors to the cargo protein?
Adaptins 1. Adaptins connect cargo protein to the transport receptors 2. Then anchors them to clathrin (which coats outside of vesicle) 3. clathrin forms vesicle around cargo proteins and dynamin pinches off vesicle
41
What are Snares and the 2 types?
Markers on vesicles and receptors on target membrane. a family of transmembrane proteins 1. V-snares (vesicle marker) 2. T-snares (target receptors) Vesicles find target by matching their v-snare to membranes t-snares, allowing them to fuse and deliver their cargo
42
is vesicle fusion thermodynamically favorable or unfavorable
unfavorable
43
What are the 2 differently pathways in Exocytosis?
1. Constitutive: default, always happening, supplies new lipids and proteins to plasma membrane 2. Regulated: Only in specialized secretion cells, vesicles don’t release their cargo to plasma membrane until receive specific signal
44
What does dynamin use to give energy to pinch off
GTP
45
what is used to disassemble clathrin coat?
ATP
46
Cells require _____ to make new membranes
Cholesterol
47
What does cholesterol travel on in the blood
LDL (Low density lipoprotein particles)
48
use cholesterol as an example for receptor mediated endocytosis
1. LDL carrying cholesterol binds to receptors on cell surfaces 2. receptor + LDL ingested then delivered to endoscopes 3. endosomes are acidic and dissociate receptor-LDL complex 4. LDL goes to lysosome and broken down to release cholesterol into cytosol, receptors sent back to cell surfaces