Biosci 201 Flashcards

(43 cards)

1
Q

What does the signal hypothesis state?

A

Proteins destined for secretion or membrane insertion are targeted to the ER during translation.

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2
Q

Who first proposed the signal hypothesis and in what year?

A

Blobel in 1971.

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3
Q

What is the pulse-chase labeling technique?

A

A method to track the movement of newly synthesized proteins using radioactive labeling.

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4
Q

What happens during the ‘pulse’ phase of pulse-chase labeling?

A

Cells are briefly exposed to a radioactively labeled molecule.

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5
Q

What occurs during the ‘chase’ phase of pulse-chase labeling?

A

The radioactive label is washed away and replaced with non-radioactive molecules.

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6
Q

What does autoradiography allow scientists to do?

A

Follow the movement of labeled molecules over time.

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7
Q

What is one piece of evidence for the signal hypothesis?

A

The relationship between larger precursor proteins and smaller mature proteins.

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8
Q

What happens to the signal peptide during protein maturation?

A

It is cleaved off, resulting in a smaller mature protein.

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9
Q

What is required for the production of mature secretory proteins?

A

The presence of microsomes.

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10
Q

What does the readout experiment prove about immunoglobulin G mRNA?

A

Proteins are translated into the ER lumen and the signal peptide is removed inside.

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11
Q

How does the presence of microsomes affect the length of the prolactin nascent chain?

A

It needs to be 130 codons long for the signal peptide to enter the ER lumen and be cleaved off.

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12
Q

What type of signal sequence do proteins destined for the ER contain?

A

An N terminus signal sequence or internal signal sequence.

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13
Q

What is the role of the signal recognition particle (SRP)?

A

It recognizes the signal sequence and pauses translation.

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14
Q

What occurs during post-translational translocation?

A

Proteins are targeted to the ER after translation.

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15
Q

What is the role of ATP in the translocation of proteins into the ER?

A

ATP hydrolysis from BiP helps pull the protein into the ER.

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16
Q

What is the nuclear localization signal (NLS)?

A

A C terminal sequence of 7 basic amino acids that targets proteins to the nucleus.

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17
Q

What is KDEL in the context of protein sorting?

A

A signal sequence that directs soluble cargo proteins back to the ER.

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18
Q

What is the process of cisternal maturation in the Golgi?

A

New vesicles from the ER fuse with the cis Golgi and mature into the trans Golgi.

19
Q

What modifications occur in the Golgi?

A

Folding, disulfide bond formation, glycosylation, and specific proteolytic cleavages.

20
Q

What is N-linked glycosylation?

A

The addition of sugars to asparagine residues on proteins occurring in the ER.

21
Q

What is the function of clathrin-adapter protein coated vesicles?

A

Transport proteins from the trans-Golgi network to lysosomes or during endocytosis.

22
Q

What is the role of dynamin in vesicle budding?

A

It hydrolyzes GTP to pinch the vesicle bud off.

23
Q

What is a dominant negative mutant?

A

A non-functional protein that is still expressed and made.

24
Q

What modification signals proteins to be targeted to the lysosome?

A

Mannose-6-phosphate modification in the cis-Golgi.

25
What are the two types of transport in the secretory pathway?
Anterograde transport and retrograde transport.
26
What mechanism retrieves proteins back to the ER?
Selective retrieval based on pH and binding to KDEL receptors.
27
What is the function of motor proteins in vesicle transport?
They transport vesicles along microtubule tracks.
28
What proteins are involved in anterograde transport to the Golgi?
COP-II coat proteins and dynein motor protein.
29
What proteins are involved in retrograde transport to the ER?
COP-I coat proteins and kinesin motor protein.
30
What is the effect of a lower pH in the Golgi compared to the ER?
It increases peptide binding to the KDEL receptor.
31
What is the role of Hsp70 in mitochondrial targeting?
It keeps pre-proteins unfolded and pulls them into the mitochondrial matrix.
32
What happens to the signal sequence after the protein enters the mitochondria?
It is cleaved off by matrix processing protease.
33
What is a dominant negative mutant?
When the protein is still expressed and made but is non-functional ## Footnote This type of mutant can interfere with the function of the wild-type protein.
34
What is the primary function of the lysosome?
Digests and recycles compartments ## Footnote This includes the breakdown of macromolecules to monomer building blocks and organelles.
35
How is the acidic pH in lysosomes maintained?
By proton pumps filled with digestive enzymes ## Footnote The acidic environment is crucial for enzyme activity.
36
Where are lysosomal proteins transported through?
RER and Golgi ## Footnote RER stands for Rough Endoplasmic Reticulum.
37
What modification signals proteins to be targeted to the lysosome?
Mannose-6-phosphate modification ## Footnote This modification occurs in the cis-Golgi.
38
What is the role of N-acetylglucosamine phosphotransferase?
Essential for the mannose-6-phosphate modification ## Footnote This enzyme is crucial for proper lysosomal targeting.
39
What happens if there is a mutation in N-acetylglucosamine phosphotransferase?
Proteins will be secreted instead of targeted to the lysosome ## Footnote This can lead to various diseases.
40
What does the trans-Golgi network contain?
An M6P receptor ## Footnote This receptor binds and recruits clathrin/AP1 coated vesicles for transport.
41
What occurs after the uncoating of vesicles in lysosomal transport?
The M6P receptor is taken back to the trans-Golgi network ## Footnote This process helps recycle the receptor for future transport.
42
What happens to endosomes as they mature?
They become more acidic and fuse to form a lysosome ## Footnote The fusion process is crucial for lysosomal function.
43
What is activated in the late endosome?
Pro-proteins are processed into digestive enzymes ## Footnote This step is necessary for the enzymes to become functional.