1.3 - Regulation of Gene Expression in Eukaryotes Flashcards

1
Q

What is the difference between transcription and translation in prokaryotes and eukaryotes?

A
  • uncoupled in eukaryotes as separated in the nuclear membrane
  • coupled in prokaryotes as no membrane to separate them
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2
Q

Explain mRNA processing in eukaryotes

A
  • 5’ end capping
  • 3’ end polyadenylation
  • splicing
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3
Q

What is 5’ end capping?

A

addition of altered nucleotide onto the 5’ end of the primary transcript that stops the strand being recognised by nucleases

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4
Q

What is 3’ end polyadenylation?

A
  • sequence at the end of gene which is recognised by specific nucleases and cleaved
  • adenines are then added
  • proteins bind to polyA tail and 5’ cap
  • protects the ends of mRNA
  • polyA tail gets shorter in translation as nucleases degrade it
  • proteins will no longer bind to poly A tail
  • mRNA looses protection
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5
Q

Is eukaryotic DNA monocistronic or polycistronic?

A

monocistronic

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6
Q

What does it mean if DNA is monocistronic?

A

every gene has its own promoter and every mRNA codes for its own protein

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7
Q

How many RNA polymerases are there in prokaryotes and eukaryotes?

A

prokaryotes - 1
eukaryotes - 3

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8
Q

What are the 3 RNA polymerase in prokaryotes?

A

Pol I - transcribe structural RNA
Pol II - transcribe all of the protein code in genes
Pol III - transcribe structural RNA

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9
Q

What is the difference in promoters between prokaryotes and eukaryotes?

A
  • in eukaryotes there is extended promoters up to 1000 bps from core promoter
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10
Q

explain transcription regulation

A
  • RNA Pol II binds to TATA box in both activated and inactive states
  • promoter proximal elements bind proteins to the RNA Pol II
  • sequences called enhancers or silencers bind either activators or repressors and then bind this to the RNA Pol II
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11
Q

What is the structure of eukaryotic promoter?

A

Promoter proximal elements
- GC - rich box - -200bp
- CCAAT - -100bp
Promoter
- TATA - -30bp

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12
Q

What is euchromatin?

A

open form of chromatin accessible to TFs

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13
Q

What is heterochromatin?

A

highly packed chromatin poorly accessible to TFs

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14
Q

Explain genes in heterochromatin and euchromatin

A

Heterochromatin
- silenced
- TFs cannot get through

Euchromatin
- active
- TFs can access

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15
Q

What is spliceosome?

A
  • ribonucleoprotein complex (made of RNA and proteins)
  • recognised the 5’ and 3’ end of exons
  • brings them together
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16
Q

How does the spliceosome do alternative splicing?

A
  • brings the 3’ end of one intron to the 5’ end of another
17
Q

What is the role of alternative mRNA spacing in sex determination of drosophila?

A
  • pre-RNA == double sex - has everything for both sexes
  • DNA binding domain is created which is the same in both sexes (exons 1, 2, 3)
  • remain exons are spliced in a combination that makes 2 different repressors(f = 4, M = 5, 6)
  • in females - represses male genes
  • in males - represses female genes
18
Q

Why are post-translational modifications important?

A
  • allows quick response to environmental signals - don’t wait for transcription and translation
  • most are reversible
  • energy saving
19
Q

Which enzyme phosphorylates a protein?

20
Q

Which enzyme dephosphorylates a protein?

A

phosphatase

21
Q

What is the role of protein kinases?

A
  • transfer a phosphate group using ATP to serine, threonine or tyrosine
  • as phosphate needs OH acceptor
22
Q

How does phosphorylation regulate protein-protein interactions?

A
  • protein A interacts with protein B
  • protein A is phosphorylates
  • protein A will no longer interact with protein B - may be due to size or charge
  • protein A does not interact with protein C
  • protein A is phosphorylates
  • protein A interacts with protein C - may be due to shape or charge
23
Q

What is needed for the increase and decrease of cyclin-CDKs?

A

increase - transcriptional activation
decrease - protein degradation

24
Q

How do cells degrade proteins that regulate the cell cycle?

A
  • ubiquitin is added to protein’s lysines that are to be degraded
  • more ubiquitin can be attached to the first lysine
  • proteasome then recognises ubiquitin and degrades the protein
25
What is ubiquitin?
- short 76 amino acid peptide that can be attached to lysines - it contains lysines so they can attach to themselves
26
What is a proteasome?
- Huge protein complex shaped like a barrel - ubinquinated proteins are degraded by it
27
Explain post translational modification in bacteria
they do not have it
28
Explain protein degradation in bacteria
- signal peptide attached to substrate - adaptor protein recognises this and binds to the signal peptide - adaptor proteins then bring the substrate to proteases where it is degraded - bacteria have multiple proteases
29
Name 8 model organisms
- M. musculus - D. rerio - X. tropicalis - D. melanogaster - C. elegans - E. coli - S. ceravisae - A. thaliana
30
name 9 requirements of model organisms
- easy to grow and maintain in a lab - short generation time - large number of offspring - well studied genome - efficient manipulation of genomes - researchers can share strains / genetic constructs - no ethical concerns - decreased complexity compared to humans - well suited to study fundamental biological processes conserved in all eukaryotes
31
Explain how phosphorylation cascades work
- kinase is activated - phosphorylates more kinases - these phosphorylate more kinases - which then phosphorylate the protein