Ch 10-nucleosomes, Chromatin, And Chromosome Structure Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Chromatin

A

Chromosome material, consists of both DNA and protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Histones

A

The family of basic proteins that associate tightly w/DNA in the chromosomes of all eukaryotic cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Nucleosomes

A

In eukaryotes, the structural unit for packaging chromatin, consists of a DNA strand wound around a histone core

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Cross linking

A

The use of a small chemical agent w/two reactive groups to covalently link molecules that are in close proximity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Histone octamer

A

The complex of 2 copies of each of the four core histones the forms the histone core of nucleosome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Histone core

A

H2A, H2B, H3, H4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Histone fold motif

A

A protein structural motif formed from 3 alpha hélices connected by two loops. Histone diners are instrumental in the tight wrapping of the DNA helix around the histone core in nucleosomes.
each histone contains a histone-fold motif

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Histone tails

A

The flexible, disordered N-terminal ends of the histone proteins that comprise the histone core. These ends protrude from the nucleosome and contact adjacent nucleosomes
-sp1 is no effective in presence of higher levels of H1 (think about pic of gel)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Linker histone

A

H1, binds to the linker DNA adjacent to the nucleosome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

30 nm filament

A

A higher-order if nucleosomes seen in condensed chromosomes

-tails are required

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

2 models for nucleosome arrangement in 30 nm filament:

A

1) solenoid model

2) zigzag model

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Solenoid model

A

Nucleosome adopts a spiral shape, in which the flat sides of adjacent nucleosome disks are next to each other. Linker DNA is thought to bend in filament in this model

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Zigzag model

A

Zigzag histone pairs stack on each other and twist about a central axis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Chromosomal scaffold

A

Proteinaceous residue after extraction of histone from chromosomes, consisting mainly of SMC proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Nucleoid

A

In bacteria, the nuclear zone that contains the chromosome but has no surrounding membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Chromatin remodeling complex

A

A protein complex with ATPase activity that translocates nucleosomes among the DNA making certain regions of DNA more or less accesible to transcription factors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Histone modifying enzymes

A

A class of enzymes that covalently modify the N-terminal tails of histones

18
Q

Epigenetic inheritance

A

The inheritance of characteristics acquired by means that do not involve the nucleotide sequence of the parental chromosomes

Ex: covalent modifications of histones

19
Q

Histone chaperones

A

Acidic proteins required for the assembly of histone octamers on DNA

-bins either H3 -> H4 or H2A -> H2B

20
Q

Histone acetlytransferases (HATs)

A

Acetylate Lys residues

21
Q

Histone deacetylases (HDACs)

A

Remove acetyl groups from histones

-usually results in transcriptional repression

22
Q

Bromodomain

A

A protein structural domain that recognizes and binds to certain acetylated lys residues in proteins

  • open
  • lys residues un larger multi protein complex, ie: chromatin remodeling complex
  • histone tail modification
  • stabilized open state
23
Q

Chromodomain

A

A protein structural motif that recognizes and binds methylated lys residues in proteins

  • stabilized closed state
  • methylation can result in activation or deactivation depending on the aa and location
24
Q

Histone code

A

A hypothetical code in which successive covalent modifications of histone tails and DNA trigger chromatin remodeling and transcriptional activation events

25
Q

Which amino acid residues predominate in the histone octamer and why?

A

Lysine and arginine predominate because they are positively charged

26
Q

What is linker DNA?

A

The DNA not wrapped around the histone octamer and served as a linker between nucleosomes, to which H1 binds

27
Q

How many base pairs does linker DNA have?

A

20-90 bp

28
Q

Approximately how much DNA is wrapped around a histone?

A

200 bp

  • the DNA sequence influences how the DNA can wrap around the histone. A-T rich regions alternating with G-C rich regions allows the DNA to naturally bend around the histone structure
  • histone octamers assemble particularly well with sequences where 2 or more A-T base pairs are staggered at 10bp intervals because DNA is naturally bent
29
Q

How do histone tails influence chromosome condensation? What are the potential effects of modifying the histone tails?

A
  • the unstructured Gail (N-terminus) is able to interact with neighboring nucleosomes
  • chemical modifications to the tails affect how the nucleosome binds DNA
  • required for filament formation
  • tails are flexible, but don’t contribute strength to DNA binding. They form intermolecular contacts with nucleosome particles into a higher order chromatin structure. The tighter the inter nucleosome connections mediated by the histone tails, the less accessible DNA is to transcription factors and other proteins
30
Q

How does H1 differ from the other histones? How does it associate with DNA?

A
  • H1 is a linker histone
  • H1 has DNA binding regions associated with its globular domain
  • H1 controls the location of the entrance and exit of the DNA which is associated with the nucleosome; plays a role in transcription regulation
  • removal of H1 causes the chromatin to be looser
31
Q

What is the function of Sp1? How is the function influenced by the presence of histone H1?

A
  • Sp1 activates transcription
  • activators are not required for transcription
  • presence of histones do not inhibit transcription
  • darker bands means you have more transcripts
  • H1 can outcompete the effects of an activator
32
Q

How do nucleosomes play a role in transcriptional regulation?

A

Nucleosomes generally repress transcription by sterically preventing the access of regulatory proteins to promoter sequences

-H1 participates in this activity by stabilizing the nucleosomes on the DNA and promoting higher-order chromatin structure that further compacts nucleosomal DNA

33
Q

What is the function of the chromatin remodeling complex (CRC)?

A
  • slide nucleosomes
  • remove the nucleosome
  • replace the nucleosome
34
Q

What is the function of histone modifying enzymes (HME)? What is the difference between cis acting and trans acting histone modifying enzymes?

A

HME affect chromatin structure:

  • cis: directly acts (no middle man)
  • trans: uses a secondary (intermediate protein)
  • histone modifying proteins stick methyl groups to loosen DNA strands

Cis: closed-open

35
Q

3 possible results from the action of the chromatin remodeling complex (CRC):

A
  • eject the nucleosome
  • move the nucleosome
  • change out the variants
36
Q

Where on the histone do the majority of modifications occur?

A

Histone tails

37
Q

Would histone acetyltranserases (HATs) be an example of of a CRC or HME?

A
  • HATs modify histone subunits and acetylate specific residues in a histone tail
  • acetylation of lysine residues
  • acetylation = activation
  • methylase
  • cis interactions are histone modifying enzyme
  • HAT would be an HME
38
Q

What are the different types of modifications that have been observed on histones?

A
  • acetylation of lysines
  • methylation of lysine, arginine
  • phosphorylation of serine
  • ubiquitination of lysine
39
Q

Acetylation of specific lysine residues by HATs results in the activation of transcription. Why might the attachment of an acetyl group to a lysine have this effect on transcription?

A

Acetyl groups can be added to lysine to neutralize the positive groups on histone and loosen the DNA

40
Q

Are histone modifications reversible?

A

Yes

41
Q

Since both marked and unmarked nucleosomes are distributed between the replicated strands of DNA how can this result in the passing of the message by CRC?

A
  • marked is modified by DNA
  • more acetylated histones have a “louder” message to pass on
  • CRC (bromodomain HAT in figure) detect acetylated histones and makes all histones acetylated and can actively transcribe