Lecture 10 Flashcards

1
Q

What does transcription do?

A

makes an RNA copy of DNA

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2
Q

What RNA transcribes most rRNA genes?

A

RNA polymerase 1

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3
Q

What RNA polymerase transcribes all protein-coding genes, miRNA genes, plus genes for other noncoding RNA’s?

A

RNA polymerase 11

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4
Q

What RNA polymerase codes tRNA genes, 5s rRNA genes and genes for many other small RNA’s?

A

RNA polymerase 111

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5
Q

What form of rna carries amino acids for translation?

A

tRNA

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6
Q

What rna codes for proteins?

A

mRNA

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7
Q

What rna is involved in gene expression?

A

micro RNA

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8
Q

What rna form the core of the ribosome’s structure and catalyze protein synthesis

A

Ribosomal RNA

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9
Q

Can RNA act as an enzyme (ribozyme), catalyzing chemical reactions?

A

yes

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10
Q

What initiates transcription to happen?

A

promoter

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11
Q

What is the TATA box?

A

is contained in the promoter and recruits general transcription factors

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12
Q

What is the role of the general transcription factors?

A

Seperate the double stranded DNA, allowing RNA polymerase II access to the template strand

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13
Q

What is it called when removing an intron?

A

splicing

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14
Q

What is the region called that has been spliced

A

splicesome

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15
Q

What does it mean when the mRNA is capped, polyadenylated, and spliced?

A

Ready for export out of the nucleus

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16
Q

What happens during translation?

A

Translation decodes the mRNA and producing the corresponding protein

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17
Q

What does translation require?

A

mRNA
Ribosome
aminoacytl-tRNA

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18
Q

What is the largest and abundant protein complexes in cells?

A

Ribosome

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19
Q

What type of RNA does ribosomes have?

20
Q

What links the proper amino acid to the corresponding tRNA?

A

tRNA synthase

21
Q

What enzyme is highly specific?

A

tRNA synthase

22
Q

what happens at the A site?

A

first binding site for aminoacyl-tRNA

23
Q

What happens in the P site?

A

tRNA linked to the polypeptide

24
Q

What happens at the E site?

A

Exit site for the tRNA

25
What is the mRNA ribosome complex called?
polysomes
26
What does polysome analysis indicate?
Translation activity of cells
27
What end of the protein starts folding as soon as it emerges from the ribosome?
N -terminal
28
Cotranslational folding of proteins only occurs to what type of proteins?
less complex proteins
29
What is the role of a molecular chaperone?
Help with protein folding
30
What do chaperones require?
ATP
31
What is the endoplasmic reticulum functions?
- protein translocation - protein folding - protein glycoslytion - protein quality control - calcium iron storage
32
What is the structure of the ER?
Membrane network, distributed by microtubule interactions
33
What materials are translated at the ER?
Transmembrane proteins and soluble lumenal proteins
34
What ensures proper insertion into the membrane or delivery into the lumen of the ER?
Ribosome linkage with protein translocator
35
What is the n terminus?
lumenal
36
What is the C - terminus?
cytosol
37
Where are the n and c termini located?
cytoplasm
38
What happens during N-linked glycosylation?
Modification of an amino group
39
What happens in o-linked glycosylation?
Modification of OH group
40
Most proteins that are translated and translocated at the ER become what?
glycosylated (both soluble and transmembrane proteins)
41
What does glycosylation increase?
Increase stability of secreted proteins
42
Why is the glycosylation of surface proteins important?
Important for recognition of self vs foreign (immune system)
43
Where do newly synthesized proteins fold?
In the ER
44
What is allowed to leave the ER?
Only folded proteins - unfolded proteins remain in the ER with chaperones
45
What happens to proteins that are not properly fold in to the ER?
They are retro translocated to the cytoplasm, ubiquitinated and degraded by the proteasome
46
What is retrotranslocation mediated by?
By the same translocator protein that allows for protein import into the ER