Section 5 - Intracellular Traffic and Energy Conversion Flashcards
How much total membrane does the ER take up?
50%
True or false: the ER is connected to the nuclear membrane
True: it extends from the nucleus into the cytosol
What are the functions of the ER?
Production of transmembrane proteins, secreted proteins, lipids, and calcium storage
What is the ER composed of?
Tubules and membranous sacs
Where is the ER the densest?
Near the nucleus
Where is the ER the least dense?
In the cytosol (away from the nucleus)
True or false: the ER in mammalian cells is the same as the ER in plant cells
False: they have very different structures
True or false: the entirety of the ER has the same function
False: different regions of the ER can be specialized for different functions
What is an example of a specific region of ER having a specialized function?
Rough ER
What is rough ER?
ER with attached ribosomes
What is smooth ER?
ER without ribosomes
What is co-translation?
When proteins are transported to the ER during translation
Is the rough ER constantly rough?
No. The ribosomes associate and dissociate from the ER, thus changing it to rough or smooth
True or false: ribosomes sit on the ER, waiting for mRNA to come
False: they are assembled in the cytosol and translocated to the ER
How does the rough ER become rough?
By the ribosome assembling in the cytosol, and then moving towards the ER
What is the function of smooth ER?
Transporting synthesized proteins / lipids to other regions of the cell (golgi)
Where is rough ER most likely to be found?
Closer to the nucleus
Why is rough ER found more commonly closer to the nucleus?
That is where mRNA is most likely to be found
What is the function of calcium in the cell?
Act as initiators for many biological functions
Why is calcium kept in the ER?
Keep cytosolic concentration low for proper function (proper cell signaling)
What is the specialized ER in muscle cells important for?
Contraction
How does the ER sequester calcium?
Through calcium binding proteins and calcium channels
What is needed on a polypeptide to direct it to the ER?
A signal sequence
Where are transmembrane proteins made?
Embedded in the ER
Where are water-soluble (secreted) proteins made?
In the ER lumen
What cleaves the signal sequence?
Signal peptidase
What does signal peptidase do?
Cleave the signal sequence off of a polypeptide
What is a translocater?
Where the growing protein in the ER is held
What does SRP stand for?
Signal recognition particle
What does the SRP do?
Move the ribosome from the cytosol to the ER
How does the SRP move a ribosome from the cytosol to the ER?
It binds to the signal sequence and an SRP receptor found on the ER membrane
What is the structure of SRP?
Proteins and RNA
True or false: the protein continues translating as it is moved from the cytosol to the ER
False: translation is halted by the SRP
Why does the SRP halt translation?
To ensure that it reaches the ER first so it can be processed correctly before continuing
What would happen if the SRP did not halt translation?
The protein would be misfolded (cassette tape)
What does an SRP do once it is bound to an SRP receptor?
It moves the polypeptide into a translocator
What are the parts of an SRP molecule?
Signal sequence binding pocket, hinge, and translational pause domain
Where is SRP most likely to be found?
Close to the nucleus
What happens to the SRP and SRP receptor after the polypeptide is in a translocator?
It gets recycled (it can be used again)
What is the structure of a ribosome in the cytosol (before translation)?
Dissociated subunits
What is the structure of the translocator?
A pore type structure
What is needed for the translocator to function properly?
A plug
What is the significance of the plug in the translocator?
Prevents the mixing of cytosol and ER lumen contents
What displaces the plug in the translocator?
The signal sequence
What happens when the plug is displaced in the translocator?
The growing polypeptide can be fed into the translocator into the ER lumen
What is the structure of the translocator in the closed position?
Hinge is closed, with a plug
What is the structure of the translocator in the open position?
The signal peptide is holding the hinge open, the plug is displaced, and the polypeptide can be fed through the pore
If a polypeptide sequence only has a start sequence at the end, what can you say about the protein?
It is a soluble (secreted) protein
For a soluble (secreted) protein, what sequence(s) does it have?
A start transfer sequence
For a multipass transmembrane protein, what sequence(s) does it have?
A start transfer sequence and a stop transfer sequence
What does a stop transfer sequence do?
Moves the polypeptide out of the translocator, and continues translation in the cytosol
True or false: the start transfer sequence can be cleaved
True: if it is at the end of a polypeptide, it can be cleaved
True or false: the stop transfer sequence can be cleaved
False: it must remain embedded in the membrane
What is the phobicity of the stop transfer sequence?
Hydrophobic
Why must the stop transfer sequence be hydrophobic?
It stays embedded within the membrane
True or false: a start transfer sequence can be found at the start or middle of the polypeptide
True: it can be in either location
True or false: a stop transfer sequence can be found at the start or middle of the polypeptide
False: it can only be in the middle of the polypeptide
True or false: the N-terminal of a polypeptide is always in the ER
False: this direction can be changed depending on the specific protein
What determines the direction of the start transfer sequence if it is in the middle of the polypeptide?
The positive and negative ends of the start transfer sequence must line up with the membrane
What side of the membrane does the positive side of the start transfer sequence line up with?
The positive side
How come the positives of the membrane and the start transfer sequence are together?
It is similar to a capacitor (like charges line up at opposite sides of the membrane)
Which leaflet of the cell membrane is more positive?
The external leaflet (compared to the internal leaflet)
For a single pass protein, where is the start sequence found?
At the beginning of the polypeptide
For a multi pass protein, where is the start sequence found?
In the middle of the polypeptide
What sequences are needed to create multi pass proteins?
Pairs of start and stop sequences
Which sequences will signal peptidase cleave?
Start signal sequences at the beginning of the polypeptide
Which sequences will signal peptidase not cleave?
Start and stop signal sequences in the middle of the polypeptide
True or false: a start sequence can be unpaired to a stop
True: it does not need a stop
True or false: a stop sequence can be unpaired to a start
False: every stop requires a start
What must the charge be between a start and stop sequence?
Negative
Why must the charge between a start and stop sequence be negative?
It needs to align with the cell membrane charge gradient
True or false: one translocator is used per polypeptide
False: multiple translocators can be used
True or false: proteins that come off of the ribosome are functional
False: they need to be processed post-translation to be functional
Where are most proteins processed after translation?
The ER
What does disulfide isomerase do?
Catalyzes the formation of the disulfide bond
Where is disulfide isomerase found?
In the ER lumen
For most loops in a transmembrane protein, are they small or large?
Small
For most tails in a transmembrane protein, are they small or large?
Large
If the loops of a transmembrane protein are large, what can you say about the loops?
They are in an organized structure (alpha helix, beta sheet, etc.)
What does oligosaccharyl transferase do?
Adds sugars to the growing polypeptide
What is the function of sugars on proteins?
Help with folding by assisting chaperone proteins
How do chaperone proteins use sugars?
If the sugar looks a certain way, then the protein should be folded correctly (on-folding pathway)
True or false: chaperones physically fold the polypeptide into the correct shape
False: they only check if it is folded correctly
What drives protein folding?
Thermodynamics
What happens if the chaperone / sugar pathway starts a perpetual loop?
It will get signaled for degradation
What pathway is used to degrade a protein?
The ubiquitin pathway
What is the purpose of the ubiquitin pathway?
It is a proteolytic pathway (break down misfolded proteins)
How can a misfolded protein signal for its own degradation?
The misfolded protein can activate a receptor to make a transcription factor, which creates more chaperones to help folding