Lectures 16-17 Flashcards

1
Q

Why does gene expression need to be controlled?

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2
Q

What is the main way genes are regulated? What are housekeeping genes? What are regulated genes?

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3
Q

Regulation of gene expression in both eukaryotes and prokaryotes requires what 2 general categories of regulators? What are examples of each?

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4
Q

Single genes produce what kind of mRNAs? Operons produce what kind?

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5
Q

Why study operons?

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6
Q

In E. coli what is the preferred carbon source? Genes for metabolizing other sugars are only present when?

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7
Q

What does the lac operon in E. Coli have genes that encode for? What is the expression of the lac operon controlled by? When is the lac operon fully expressed?

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8
Q

What are the major differences in gene regulation from prokaryotes to eukaryotes?

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9
Q

What experience chromosome inactivation and chromosome compensation?

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10
Q

What is DNA methylation? What is a DNMT? What are methylated cytosines responsible for? Where does it alter the structure of cytosines?

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11
Q

What is chromatin remodeling and how does it work? Are chromatin remodelers repressors or activators of genes?

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12
Q

Describe what histone acetylation/deacetylation does.

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13
Q

When does the highest level of transcription occur?

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14
Q

Where do enhancers and silencers act?

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15
Q

Activator proteins have what 2 domains? Where do they act?

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16
Q

What are the 3 ways repressor proteins prevent transcription?

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17
Q

Micro RNAs do what? How do RNAi’s silence genes?

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18
Q

What is siRNA therapy? What disease is it used to treat? How many drugs are approved by the FDA?

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19
Q

How is translation regulated? How do cells respond to stress? What is eIF2? What does it do?

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20
Q

What are some modifications made post-transcriptionally? What are chaperone proteins? What are the fates of misfolded proteins?

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21
Q

What are disulfide bridges? What do they link/ are they reversible? What are PDIs\ where are they found? What is protein cleavage? What do they produce? Are cleavage reactions reversible?

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22
Q

What are some protein chemical modifications? When do they occur?

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23
Q

What is phosphorylation? What do phosphatases do? What is acetylation? What is methylation?

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24
Q

What does hydroxylation do? What is it catalyzed by? What is lipidation? What does lipidation do?

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25
Q

What does GPI anchoring do? What does glycoslyation do?

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26
Q

What is protein targeting in eukaryotes? How is it accomplished? What are the 6 steps? Proteins going where are translated in the ER? Proteins going where are completely translated in the cytoplasm?

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27
Q

What happens when proteins within the cell are no longer needed? Lysosomes degrade proteins from where? The proteasome degrades proteins from where and how?

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28
Q

What are the steps in degrading a protein by the proteasome? How is Ubiquitin involved? What is Von Hippel-Lindau Disease? What is Bortezomib?

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