Exam #3 Flashcards

1
Q

What regulates gene expression?

A

Gene expression is regulated by any mechanism that controls how much mRNA or protein for a given gene is present in a cell

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2
Q

What are some controls for gene expression at translation?

A
  • Regulation of translation is largely controlled at the initiation step.
  • These mechanisms black access of the ribosome and the initiator tRNA to the AUG (initiation site)
  • These mechanisms often rely on secondary structures produced by the mRNA transcript itself
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3
Q

What happens when you bind a translation repressor protein to the ribosome-binding site on mRNA?

A

No protein is made

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4
Q

What happens when you increase the temperature of the ribosome-binding site on mRNA?

A

Protein is made

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5
Q

What happens when there is low iron concentration?

A

Iron regulatory protein (IRP) binds to the iron-response element (IRE) to prevent translation

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6
Q

What happens when there is high iron concentration?

A

Free iron binds to the Iron Regulatory protein (IRP), causing it to dissociate from the IRE, allowing the translation of the mRNA to form ferritin

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7
Q

What are the basic steps of gene expression?

A
  • DNA
    1) Transcriptional control
  • RNA transcript
    2) RNA processing control
  • mRNA
    3) RNA transport and localization control
  • mRNA
    4) mRNA degradation control –> Inactive mRNA
    5) Translation control –> protein
    6) Protein activity control
  • Inactive or active protein
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8
Q

What is the general mRNA half-life in bacteria and more abundant proteins?

A

Bacteria: <2-3 mins
More abundant: longer than bacteria

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9
Q

Eukaryotic mRNA is degraded by two general mechanisms, which are…

A

1) Decapping and rapid 5’ > 3’ degradation

2) Shortened poly-A tail and rapid 3’ > 5’ degradation

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10
Q
A
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11
Q

What is miRNA? What does it do?

A
  • Short RNA sequences that do not code for proteins
  • miRNA direct the action of the RNA-induced silencing complex (RISC) to mRNA with complementary sequences to the miRNA
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12
Q

What can miRNA induce?

A

miRNA can induce mRNA degradation

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13
Q

What is RNA interference (RNAi)?

A
  • A cellular defense mechanism also used by scientists
  • Works similarity to miRNA
  • Perhaps first discovered in petunia
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14
Q

What does siRNA do in RNAi?

A

siRNA than function like miRNA with RISC to chew up complementary RNA molecules in the virus genome

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15
Q

What can scientists do to a gene they want to inhibit?

A

Scientists can introduce dsRNA for the gene they want to inhibit and let Dicer and RISC do the work

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16
Q

What DNA-binding proteins guide nucleases?

A
  • Zinc-finger nucleases (ZFNs)
  • Transcription-activator like effector nucleases (TALENs)
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17
Q

What kind of RNA guides nuclease?

A
  • CRISPR-Cas9 system
18
Q

What is CRISPR-Cas9? What are the parts of it?

A
  • It is an adaptive immunity in bacteria
  • CRISPR: clustered regulatory interspaced short palindromic repeats
  • Cas9: CRISPR associated 9 (nuclease)
19
Q

When all else fails, ______ the darn thing!

20
Q

What is a proteasome?

A

An abundant protease that only proteolyzes proteins marked for destruction with a polyubiquitin tag.

21
Q

What happens to damaged or otherwise unwanted proteins?

A

They are degraded by the proteasome

22
Q

What does E1-E2-E3 ubiquitin ligase do?

A

It adds ubiquitin into other proteins

23
Q

What is E1?

A

ubiquitin activating enzyme

24
Q

What is the E2-E3 complex?

A

ubiquitin ligase

25
What do E1 and E2-E3 complex do when they're together?
The proteins recognize degradation signals in proteins and add a polyubiquitin chain
26
What kind of polyubiquitin chain does E1-E2-E3 add to?
- Adds mostly to lysine 40 - Not as much lysine 63
27
What is the polymer of an amino acid?
Protein
28
What does a protein's unique animo acid sequence determine?
It determines its structural and chemical properties
29
What are the chemical natures of the 4 side chains?
- Positively charged AA - Negatively charged AA - Polar AA (hydrophobic) - Non-polar AA (hydrophilic)
30
What is the Hydrophobic effect on proteins?
The aversion of hydrophobic resides to water is a major force in driving protein conformation
31
What is the significance of the shape of a protein?
the specific shape of a protein determines what binds to it (interacts with it), which determines its function
32
What are disulfide bonds?
They are covalent bonds between sulfur atoms in cysteine side chains
33
What are the 4 types of protein structure? What are their function?
- Primary: amino acid sequence - Secondary: common ‘shapes’ formed by small stretches of amino acids (ex. α-helices, β-strands/sheets) - Tertiary: overall structure, larger domains formed by combinations of secondary elements - Quaternary: assembly of proteins into large multi-protein complexes
34
What happens to side chains when glucose is introduced?
The side chains all form h-binds with glucose, causing the protein to fold around the glucose molecule
35
Proteins are modular. What does this mean? Can you give any examples?
- Different domains have different functions - Ex: catalytic, regulatory, structural, interactions
36
What are the major enzyme classes?
- DNAase, RNAase, proteinase, lipase – hydrolytic cleavage of substrate polymer - Polymerase – promotes formation of DNA / RNA polymers - Kinase / Phosphatase – add / remove a phosphate groups to molecules, usually proteins. - ATPase / GTPase – hydrolyze ATP / GTP nucleotide triphosphates to ADP / GDP.
37
What do DNAase, RNAase, proteinase, lipase do?
Hydrolytic cleavage of substrate polymer
38
What does Polymerase do?
Promotes formation of DNA / RNA polymers
39
What does Kinase / Phosphatase do?
Add / remove a phosphate groups to molecules, usually proteins.
40
What does ATPase / GTPase do?
Hydrolyze ATP / GTP nucleotide triphosphates to ADP / GDP.
41
What are some consequences of phosphorylation?
- There's now a neg. molecular charge, meaning a molecular change to the molecule -