Details Flashcards

1
Q

Oxidative Damage

A

C -> T

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2
Q

Base Alkylation

A

G -> O6-meG, bp w/ T

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3
Q

Base Adduct

A

G-BPDE bp w/ A

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4
Q

Steps of Excision

A

Recognition, Endonuclease, Exonuclease, DNA Pol, DNA Ligase

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5
Q

BER

A

Glycosylase recognizes and remove incorrect base

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6
Q

NER

A

TFIIH unwinds and endonuclease cuts backbone 30 bp around lesion. Can be Global or txn-coupled

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7
Q

Mismatch Repair

A

MSH and MLH recognize and endonucleate. Helicase unwinds. Recognize nicks in lagging and leading new strands. RNAase H2 exonucleates)

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8
Q

Avery, McCloud and McCarty

A

DNA hereditary material, Transformed pneumococcus from R (benign) to S (deadly)

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9
Q

Tm

A

Melting temperature. Where 50% of the DS are melted

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10
Q

CpG Sequences

A

Palindrome like C-G combinations. Gets methylated.

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11
Q

Processive/Distributuive

A

Processive is carried out by one enzyme while distributive uses multiple enzmes

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12
Q

p53 significance

A

Major regulatory txn factor (Cancer

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13
Q

RNA Polymerase parts

A

Clamp, jaws, bridge helix. C terminal domain important for splicing, elongation factors and can be phosphorylated

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14
Q

TATA box

A

Exists in promoter and bound by tata binding proteins

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15
Q

TFIIH, CDK7

A

Phosphorylates CTD of RNA Polto help with promoter clearance and unbind preinitiation complex

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16
Q

Capping Transcript

A

7-methylGTP bound reversibly to 5’ end. CBC binds 7me within nucleus and transports to cytoplasm, also plays role in splicing, and starting poly a tail. eIF4E binds in nucleus to initiate tln. No eIF4E causes degradation of mRNA

17
Q

Consensus Sequences

A

5’ splice site: GA
3’ splice site: UG
Termination: AAUAAA

18
Q

Splicing

A

Cross exon proteins designate boundaries.
Step 1: 2’ –OH of branch point attacks 3’ P on 5’ splice site
Step 2: 3’ –OH attacks 5’ P of the 3’ splice site

19
Q

Poly Adenylation

A

After AAUAAA. Stability, protection, transport, circularizing. Long poly A tail can keep mRNA around longer. Different poly A tails can produce bound and free IgM

20
Q

Homeodomain

A

Helix Loop Helix. composed of 3 alpha-helices. Regulates growth and development

21
Q

Zinc Finger

A

3 loops with cysteine and zinc. Dimerize

22
Q

Basic Leucine Zipper

A

Leucine residues and dimers

23
Q

Helix-Loop-Helix

A

Hydrophobic residueswith

24
Q

Repressor Action

A

Competitive binding of the same enhancer
Bind to and inactivate an activator
Bind directly to other txn factors to inhibit initiation

25
Trans acting factors (Proteins)
Reg nuclear entry Reg amount of txn factor in cell Reg binding to DNA Phosphorylation of DNA-BP to change properties
26
IkB binds NF-kB and stops entry into nucleus
Phosphorylation of IkB leads to ubiquitination and degredation The freed NF-kB moves to nucleus to initiate inflammation Aspirin inhibits phosphorylation of IkB and stops inflammatory response
27
Beta-Catenin
Beta-Catenin is regulated through APC binding and causing degredation Wnt signal inactivates APC allowing for Beta-Catenin to act as txn factor and upreg Wnt genes APC represses tumors in colon
28
P53 can activate the apoptotic or growth suppressor pathways
MDM2 degrades p53 and can reduce cellular protection from mutations Present in cancers that don’t undergo apoptosis
29
Creb Regulation
Creb is phosphorylated which allows binding to DNA and recruitment of CBP (a HAT)
30
Bacterial initiation of translation
IF1 binds A site of small subunit IF3 binds small subunit IF2 binds formylmethionine tRNA to the P Hydrolysis of GTP on IF2 releases initiation factors and binds large subunit
31
Eukaryotic initiation of translation
Ribosome binds cap and scans to first AUG | Kozak sequences can provide context and up/down regulate which genes are tln
32
Missense Mutation
Change AA
33
Silent Mutation
No change in AA
34
Nonsense Mutation
Change to stop codon
35
Sense Mutation
Change to miss stop codon
36
Psuedoknots
Frameshift recoding by slipping tRNA 1 BP
37
Cap-independent binding
Viral mRNA can tln without cap binding proteins
38
apoB
mRNA is modified after txn to cause nonsense mutation
39
Protein Chaperones
HSP 70, 40, Chaperonin