Lectures 16-17

Question 1

Why does gene expression need to be controlled?

Answer 1

Question 2

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

Answer 2

Question 3

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

Answer 3

Question 4

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

Answer 4

Question 5

Why study operons?

Answer 5

Question 6

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

Answer 6

Question 7

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?

Answer 7

Question 8

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

Answer 8

Question 9

What experience chromosome inactivation and chromosome compensation?

Answer 9

Question 10

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

Answer 10

Question 11

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

Answer 11

Question 12

Describe what histone acetylation/deacetylation does.

Answer 12

Question 13

When does the highest level of transcription occur?

Answer 13

Question 14

Where do enhancers and silencers act?

Answer 14

Question 15

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

Answer 15

Question 16

What are the 3 ways repressor proteins prevent transcription?

Answer 16

Question 17

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

Answer 17

Question 18

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

Answer 18

Question 19

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

Answer 19

Question 20

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

Answer 20

Question 21

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?

Answer 21

Question 22

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

Answer 22

Question 23

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

Answer 23

Question 24

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

Answer 24

Question 25

What does GPI anchoring do? What does glycoslyation do?

Answer 25

Question 26

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?

Answer 26

Question 27

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

Answer 27

Question 28

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

Answer 28