aa side chain modifications
Misc.
Damage Repair
T/F
Chromatin remodeling
100

Number of times lysin can be methylated

3

100

DNA elements that make up the largest % of the human genome

LINEs

100

Pathways that can be involved in repairing stalled replication forks

NER, BER

100

Heterochromatin is highly condensed and associated with active transcription 

False. Heterochromatin restricts transcription from taking place since it is highly condensed.

100

Chromatin that allows gene transcription

Euchromatin

200

Modification that adds a negative charge to a histone

phosphorylation 

200

DNA region that prevents heterochromatin from spreading to active genes

Barrier DNA

200
Structure that forms when DNA strands exchange during recombination

Holliday junction

200

Barrier DNA prevents the spreading of heterochromatin

True

200

Stabilizes zigzag chromatin fiber structure

Histone H1 and histone tail interactions

300

Effect that acetylation of lysine has on histones

Removes positive charge, loosens chromatin

300

HMTs

adds methyl groups to lysine residues

300

Process that can cause gene conversion

homology-directed repair

300

Chromatin remodelers use GTP hydrolysis to reposition nucleosomes

False. Chromatin remodeling complexes use ATP hydrolysis to catalyze repositioning of nucleosomes.

300

Histone variant that replaces H3 at centromeres

CENP-A

400

Enzyme family that adds acetyl groups to histones

HATs

400

HDMs

removes methyl groups from histones

400

The main function of the FA pathway

Repair inter strand cross-links

400

Number of nucleosomes per ATP-dependent remodeling complex

5

400

Heterochromatin

highly compact, transcriptionally inactive chromatin

500

Enzyme family that removes acyl groups, promoting chromatin compaction

HDACs

500

Primary function of histone H1

Binds linker DNA to compact chromatin

500

Structure formed after strand invasion during HDR

D-loop

500
H3.3 is associated with transcriptional activation

True

500

Reason why histone tails are intrinsically disordered

to interact with other proteins

M
e
n
u