Topic 2, Lecture 2 Flashcards

1
Q

Nucleosome are static or dynamic?

A

dynamic

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2
Q

why are they stated to be dynamic

A

bc they are (breathing) not tightly wrapped

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3
Q

how long in milliseconds do nucleosomes exist wrapped and unwrapped?

A

250 milliseconds wrapped
10-50 milliseconds unwrapped

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4
Q

at what rate are nucleosomes unwrapped?

A

from each end at a rate of about 4 times per second

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5
Q

If the protein has high affinity for sequence, the sequence specific DNA binding protein bind to the nucleosome when DNA is

A

unwrapped

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6
Q

cis vs trans

A

cis- before promoter region
trans- binds to neighbor to control different genes

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7
Q

promoter

A

site of general transcription factor and RNA polymerase assembly
aka pre initiation complex

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8
Q

cis-regulatory sequence- (enhancer) and how far?

A

regulatory sequence located up to 50,000 bp away from start site- controls the rate of pre-initiation assembly at the start site.

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9
Q

section of random exposure

A

binding site for sequence specific DNA binding protein

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10
Q

what is the purpose of spacer DNA

A

to provide flexibility

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11
Q

all of the other proteins located on the drawing are known at the

A

general transcription proteins and they are all non-specific

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12
Q

tata box

A

immediately upsteam from +1 site -30bp away from +1 site

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13
Q

what is responsible for decondensation?

A

transcription regulators which are
histone modifying enzymes and chromatin remodeling complexes

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14
Q

the transcription regulators are just binding sites for

A

the histone and chromatin-remodeling complex

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15
Q

what are the ways that affect chromatin structure?

A

sliding
histone- removal
histone variants

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16
Q

Chromatin remodeling enzyme

A

binds to DNA
induces association of DNA from nucleosomes
causes the nucleosome to slide , exposing specific DNA sequences
this sliding needs energy, and can be cis-regions

END GAME:

can completely disassemble
or replace via variant histones

17
Q

How do Histone variants work

A

work histone chaperones
composed of aspartate and glutamate
not a function of protein folding but just keep things apart

18
Q

Histone chaperones can do what?

A

replace histones with weaker histones for looser packing
remove whole histones or switch out bc purpose is to expose and decompose

19
Q

T/F: chromosome remodeling complexes play a critical role in the initiation of a gene transcription.

20
Q

what are transcription activators?

A

Proteins that promote the binding of additional regulators

21
Q

what do they do?

A

recruit RNA polymerase to promote
release RNA polymerase from pause

22
Q

what kind of modifications can we do to the histone tails?

A

Methylation
only lysine; leads to condensation, creates heterochromatin, addition methyl to lysine
(preserves the + charge)
acetylation
only lysine; leads to decondensation; creates euchromatin, additon of acetyl removes + charge from lysine
phosphorylation
only serine and threonine; leads to decondensation, creates euchromatin (additon of phosphate)

23
Q

what is the histone code

A

sum total of all modifications together
depends on the histone modifying enzyme that binds to the transcription factor
dimmer that controls condensations

24
Q

Histone deacetylase

A

removal of acetyl (recondense)

25
histone methyltransferase
transfer methyl to histone (lock that baby with positive charge)
26
what are the two domains of the transcription factors?
activation/ repressor domain: not-specific (no actual activation) DNA binding domain determines where binding occurs, gets activation domain to correct spot
27
what is a cofactor?
things that bind to the activation or repression domain, the activation is not specific at all, it activates wherever it is put. DNA BINDING DOMAIN is very SPECIFIC.
28
what groove does the transcription factor bind to?
major groove because there is more information present/ more potential more specificity/ tighter binding