Chapter 33 the control of gene expression in eukaryotes Flashcards

1
Q

why are there different stable cell types

A

epigonome, differences in chromatin structure and covalent modification of DNA and not that the sequence is different

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2
Q

what do transcription factors do?

A

they interact directly with the transcriptional machinery and indirectly by changing chromatin structure

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3
Q

what is a chromatin

A

the entire complex of a DNA + the associated proteins

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4
Q

histone octamer

A

two units of H2A, H2B, H3 and H4

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5
Q

nucleosome core particle

A

145 bP + histones

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6
Q

which histone binds to linker DNA

A

H1

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7
Q

what does DNA form when wrapped around the histone core

A

a left-handed superhelix

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8
Q

what parts of the DNA do the histone core proteins interact with

A

inner face of DNA especially the phosphodiester backbone and the minor groove

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9
Q

why is the DNA wrapped around histone octamer as left-handed superhelix

A

because the left-handed direction stores negative supercoils, which can be used to underwind DNA when replication or transcription takes place

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10
Q

what part of transcription factor promotes transcription and how does it do it?

A

activation domain by interacting with RNA polymerase II, or by changing local chromatin structure or interacting with proteins that lead to the interaction with RNA polymerase II

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11
Q

classes of DNA-binding proteins in transcription factors in eukaryotes

A

Homeodomains
basic-leucin zipper proteins
cys2his2 zinc finger-domains

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12
Q

how can transcription factors for example act indirectly on RNA polymerase II?

A

through mediators interactions with the activation domains of transcription factors.
mediators faciltate the phorphorylation of the carboxyæ terminal of Polymerase

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13
Q

common features between activation domains

A

1- redundant: a part of it can be deleted without loss of function

2- modular: activate transcription when paired with a variety of DNA -binding domaains

3- act synergestically: acting together much stronger effect than acting alone

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14
Q

the opposite of mediators

A

transcriptional repressors

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15
Q

combinatorial control

A

proteins affecting the patterns of gene expression

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16
Q

enhancer

A

only effective when they are found in cells expressing the regulatory proteins that bind to them

they change the local chromatin structure rather than interacting directly with the RNA polymerase

17
Q

Hypersensitive sites

A

regions adjacent to genes if transcribed are susceptible to cleavage by DNase 1 if not transccribed resistent to cleavage

18
Q

DNA-methylation causes the ….. of transcription

A

inhibition

19
Q

Which nukleotide can be methylated and describe the mechanism

A

cytosin
5-methyl group extends to the major groove and interferes with the binding of proteins that cause the stimulation of trascription

20
Q

hypomethylation

A

absence of 5-methylcytosine near the start site

21
Q

estrogen binds to and the mode of action

A

nuclear hormone receptors
Estrogen receptor
consensus sequence AGGTCANNNTGTCCT
binds as a dimer
DNA-binding domain lies at the center and consists of a set of zinc based domains bind to DNA via alpha helices inserted into the major groove.
Ligand binding site towards the carboxyl terminal

22
Q

How does estrogen receptor and related receptors induce the change in gene expression

A

by attracting coactivators upon the binding of estrogen to the receptor SRC-1 (sterioid receptor coactivator 1)
GRIP-1 (glucocorticoid receptor interacting protein 1 )
NcoA-1 (nuclear hormone receptor coactivator 1)
the belong p160 family

23
Q

Tamoxifin and Estrogen-receptor mediated pathway

A

blocks the binding of coactivators and inhibits the activation of gene expression
does that by binding to the bindings sites and thus block the normal conformational changes that lead to induce and cause the chromatin structureto change
. helix 12 can not pack into its usual position and therefore, the helix 12 will block the binding of the coactivator

24
Q

histone acetyl-transferases which histone H3

A

transfer of acetyl from acetyl-CoA to lysin
some coactivators from p160 family can also do that
H3

25
Q

what is a bromodomain

A

a domain in many eukaryotic regulatory proteins. Bind to peptides containing acetyllysine

26
Q

proteins binding to TATA-box

A

TAFS (TATA-box-binding protein associated factors)

27
Q

where are bromdomains present?

A

In TAFs and chromatin remodelling complexes/engines

28
Q

chromatin remodelling complexes how do they work and what do they need?

A

ATP hydrolysis

they shift the positions of nucleosomes along the DNA and induce other conformational changes

29
Q

how does acetylation work

A

1- reduced affinity
2- recruiting other components of the transcriptional machinery
3- shifting the positions of nucleosomes
they all activate transcription

30
Q

what removes the acetyl group from histones

and what does this cause

A

histone deacetylases

the block of transcription by increasing the affinity of the histones for the DNA

31
Q

why is excess of iron damaging

A

because there are not proteins enough to bind the iron and the iron will therefore be free to form many reactive radicals

32
Q

to what end does the IRP bind to ferritin-mRNA

A

5’ end

33
Q

to what end does the IRP bind to transferrin-mRNA

A

3’end