Amniocentesis - DNA/RNA replication/translations Flashcards

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1
Q

DNA pol I

A

prok DNA pol, poly, proof, exo 5’ to 3’

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2
Q

DNA pol III

A

prok DNA pol, poly, proof

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3
Q

DNA pol a

A

euk DNA pol, primase, poly

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4
Q

DNA pol b

A

euk DNA pol, poly, repair

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5
Q

DNA pol delta

A

euk DNA pol, primase, poly, proof on LAGGING

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6
Q

DNA pol epsilon

A

euk DNA pol, primase, poly, proof on LEADING

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7
Q

RnaseH

A

euk removal of primer during DNA pol

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8
Q

Start codon

A

AUG - meth

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9
Q

Stop codons

A

UAA, UAG, UGA

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10
Q

DNA pol gamma

A

euk DNA pol, primase, poly, proof in MITOCHONDRIA

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11
Q

Primary active sites on tRNA

A

CCA and anticodon

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12
Q

Aminoacyl-tRNA synthetase

A

Attaching AA to the sugar -OH on tRNA through ester linkage, cost equiv of 2 ATP, have proofreading

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13
Q

Prok Ribosomes

A

70S = 30S (16S rRNA+prot) + 50S (23S rRNA+5S rRNA+prot)

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14
Q

Euk Ribosomes

A

80S = 40S (18S rRNA+prot) + 60S (5.8S rRNA+28S rRNA+prot and 5S RNA from other place)

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15
Q

Ribosome sites

A

A - aminoacyl-tRNA
P - peptidyl transferase - peptide bond formation
E - exit

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16
Q

eIF2

A

euk Initiation factor 2 bound to GTP binds tRNA-met-i

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17
Q

eIF3

A

euk Initiation factor 3 bound to 40S euk smaller ribosome subunit, anti-associtation, binds to eIF2-tRNA-AA-GTP

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18
Q

eIF1 and eIF1a

A

euk Initiation factor 1 binds to eIF2-AA and eIF3-40S

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19
Q

eIF4

A

binds 5’ end to mRNA and brings into ribosomal small unit, leading to scanning of mRNA looking for first AUG, needs ATP

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20
Q

When is eIF2-GTP released?

A

When start codon is found, eIF2-GTP is hydrolyzed to eIF2-GDP and released from small subunit

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21
Q

eIF5B

A

Uses GTP to bring in large ribosomal subunit, eIF3 leaves

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22
Q

PAB

A

Poly-A binding protein, part of eIF4 that binds to poly-A tail of mRNA

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23
Q

eIF4E

A

Binds to 5’ End of mRNA

24
Q

eIF4G

A

Grabs hold of PAB and eIF4E and holds mRNA in circular form

25
Q

eIF4A

A

used ATP facilitates scanning of mRNA for AUG codon

26
Q

RAD51

A

Heterologous Repair - binds to injury and used to scan for new template

27
Q

What id the only tRNA that can go directly to the p-site?

A

Met-tRNA-i

28
Q

EF1a-GTP

A

Elongation factor 1a-GTP can recognize activated tRNA-AAs and shuttle them to a-site until correct anticodon is found, when found EF1a-GTP hydrolyzed to EF1a-GDP and released

29
Q

How is EF1a-GTP regenerated?

A

EF1betagamma facilitates release of EF1a-GDP and GTP reinteracts with EF1a, after activation EF1a-GTP can pick up another activated tRNA

30
Q

Direction of peptide formation

A

N to C

31
Q

Ribosomal peptidyl transferase

A

Ribozyme that transfers AA from carrier tRNA to alpha amino group of AA in A-site forming peptide bond

32
Q

EF2-GTP

A

Elongation factor 2 moved mRNA and dipeptidyl tRNA from A site to P site through EF2-GTP hydrolysis to GDP

33
Q

eRF1

A

recognizes stop codon by release factors and hydrolysis of peptide chain and disassembly of ribosomal protein complex

34
Q

eRF3-GTP

A

recognizes stop codon by release factors and hydrolysis of peptide chain and disassembly of ribosomal protein complex, GTP to GDP

35
Q

IF1-3

A

Prok initiation factors with same functions as eIF1-3

36
Q

Formelyn

A

Formilated meth used as start codon in prok

37
Q

Shine-Dalgarno

A

Prok 16S rRNA is complementary to SD region and when it lines up translation begins, saves energy because no scanning for start codon (save 1 ATP)

38
Q

EF-Tu

A

Prok equiv to EF1a

39
Q

EF-Ts

A

Prok equiv to EF1betagamma

40
Q

EF-G

A

Prok equiv to EF2

41
Q

RF1 and RF2

A

prok release factors that recognize STOP codons (UAA, UAG, UGA)

42
Q

RF3-GTP

A

promotes release of RF1 or RF2 in prok, and GTP is hydrolyzed to release RF3

43
Q

RRF

A

ribosomal recycling factors promotes dissociation of ribosomal complex in prok

44
Q

How is EF2-GTP regenerated?

A

EF2beta facilitates release of EF2-GDP and GTP reinteracts with EF2

45
Q

How can eIF2 be regulated?

A

Phosphorylation of eIF2 when its bound to eIF2b wont allow the complex to dissociate and eIF2-GDP cant be recharged to GTP, GLOBAL REGULATION OF TRANSLATION

46
Q

How can eIF4e be regulated?

A

eIF4e is usually bound to 4E-BP which inactivates it. Under normal conditions eIF4e is phosphorylated and then detaches to bind to 5’ end of mRNA. Regulations of phosphorylation will cause GLOBAL REGULATION OF TRANSLATION

47
Q

mRNA masking

A

complex can hide start codon and keep other interactions that would keep it from being translated. mRNA SPECIFIC REGULATION OF TRANSLATION

48
Q

ADP ribosylation of EF-2

A

Mechanisms for controlling elongation in euk.

49
Q

Recoding of UGA codon to selenoproteins

A

Change UGA to selenoproteins and presence of SECIS element prevents the stop codon from being read, specialized elongation factor

50
Q

Puromycin

A

resembles Aminoacyl-tRNA - affects both prok and euk by plugging up A-site

51
Q

Cycloheximide

A

inhibits peptidyl transferase preventing elongation in euk

52
Q

Streptomycin

A

Prevents binding at P-site by binding to 30S (S12) subunit in Prok

53
Q

Tetracyclines

A

Prevents binding at A-site by binding to 30S (S12) subunit in Prok

54
Q

Chloramphenicol

A

Inhibits peptidyl transferase to keep polypeptide from forming, affects euk mitochondria and prok because similar machinery

55
Q

Erythromycin

A

Blocks tunnel of 50S subunit in prok