Lecture 9 Slides Flashcards

0
Q

Regulatory genes

A

Turn genes on and off

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1
Q

What are housekeeping genes

A

Constitutive genes - expressed all the time

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2
Q

Four levels of regulation of gene expression

A
  1. Transcription
  2. Post transcription
  3. Translation
  4. Post translation
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3
Q

Three ways to regulate gene expression post transcription

A

RNA processing, eg splicing
Rna degradation
Rna transport, eg nuclear export

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4
Q

Half life of prokaryotic rna

A

Three minutes

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5
Q

Half life of eukaryotic rna

A

Minutes to hours

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6
Q

What does regulation depend on during translation

A

Whether or not ribosome can translate mRNA

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7
Q

Three ways to regulate gene expression post translation

A

Affect protein stability - some proteins denature easily
Some proteins are targeted for degradation
Modifications eg phosphorylation

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8
Q

Example of negative control in transcription

A

Repressing splicing so intron is not removed

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9
Q

Positive control example during transcription

A

Using an activator to make splicing happen

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10
Q

At what point in ponytail does mRNA start to degrade

A

When there are 25 or fewer adenines

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11
Q

Is mRNA decamped before degradation

A

Yes

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12
Q

In what direction does degradation happen

A

5’ to 3’

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13
Q

What initiation factors initiate translation

A

EIF4G and eIF4E

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14
Q

What enzyme degrades poly A tail

A

Deadenylase

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15
Q

What is a translation repressor protein

A

A protein that blocks the start codon AUG

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16
Q

How can a newly synthesized protein fold?

A
  1. Correctly folded without help
  2. Correctly folded with help of a molecular chaperone
  3. Incompletely folded and digested by the proteasome
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17
Q

What digests a protein that is incompletely folded

A

A proteosome

18
Q

What kind of cells have proteosomes in the cytosol

A

Eukaryotes, archea, and some bacteria

19
Q

What is Ubiquitin ligase

A

An enzyme that binds Ubiquitin

20
Q

Where is Ubiquitin added to unwanted protein

A

To side chain, ends with N terminal. Add c terminal end of Ubiquitin.

21
Q

Polyubiquitin

A

More than one Ubiquitin has been added to unwanted protein

22
Q

What happens to unwanted protein once Ubiquitin has bound to it

A

It goes to a proteosome, where it is unfolded. Ubiquitin doesn’t go in. Amino acids are recycled.

23
Q

How many amino acids in Ubiquitin

24
How many lysine residues in Ubiquitin
Seven
25
What are the two subunits of Ubiquitin ligase? What is their function.
E2- Ubiquitin transferase | e3- recognizes target protein
26
What is E1 unit
It is the carrier of Ubiquitin
27
What does E1 do with the Ubiquitin it carries
It charges E2
28
What do proteosome target proteins have
PEST motif, which is phosphorylated
29
Destruction box
Amino acid sequence required for degradation
30
n-end rule
N-terminal amino acid of a protein determines its half life (likelihood of being degraded)
31
How is Ubiquitin ligase activated
Phosphorylation by protein kinase | Allosteric transition by ligand binding or protein subunit addition
32
How is a degradation signal activated
Phosphorylation by protein kinase Unmasking by protein dissociation Creation of destabilizing N-terminus
33
Density and molecular weight of proteosome
26s | 2.5 MDa
34
Proteosome subunits
``` 19s cap 20s cylinder (active site) ```
35
What is active site of proteosome
20s cylinder
36
What does unfolding and pulling of protein throufh cylinder require
ATP
37
How does target protein attach to proteosome
At unfoldase ring
38
Contents of cap of proteosome
Ubiquitin receptor Unfoldase ring Ubiquitin hydrolase (to release Ubiquitin)
39
Shape of unfoldase ring
Hexameric
40
Is inactivation by polyubiquination reversible
No
41
Cell life cycle phasesq
Interphase - G1, S phase, G2 | M phase- mitosis and cytokinesis
42
What is cyclin
An enzyme whose concentration varies with stages of cell life cycle
43
When is cyclin concentration high? Low?
High in mitosis | Low during interphase