Exam 3 Flashcards

0
Q

Glutamine synthetase

A

AMP added and activity decreases

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1
Q

Peptidyltransferase

A

23S rRNA

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2
Q

Catabolite repression

A

If glucose and lactose are present in the environment

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3
Q

Phosphatase

A

Mediates feedback for Two Component Regulatory Systems

Always removes phosphate group at constant rate

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4
Q

Riboswitches

A

A metabolite bonds mRNA on 5’ end, hiding the Shine Dalgarno sequence, preventing translation.

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5
Q

EF-G

A

GTP used to translocate the ribosome along the strand

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6
Q

Catabolite Activator Protein

A

Bonds to CAP binding site

Only occurs when bound by cyclic AMP

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7
Q

Mutation frequency

A

Relatively rare

Every 10^9- 10^8 base pairs

DNA Polymerase has proofreading capabilities

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8
Q

Termination codons

A

3 codons

tRNA will not bind but a release factor will bind and cleave the peptide. Ribosomal subunits dissociate.

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9
Q

Antisense RNA

A

40-490 bases long (avg 100)

Has its own gene and can bind to multiple different mRNA’s

Shuts down translation by targeting strand for deletion

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10
Q

Cyclic AMP

A

Synthesized by adenylate Cyclase

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11
Q

Adenylate Cyclase

A

Synthesizes cyclic AMP

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12
Q

Why are mutations more common in Prok than Euk?

A

Less DNA

HAPLOID, so the DNA will be passed on indefinitely.

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13
Q

Release factors

A

Euk=> 1

Bact=> 3

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14
Q

Hfq protein

A

Facilitates proper RNA to RNA interaction in terms of antisense RNA

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15
Q

Mutant strain

A

Genotype will differ

Phenotype may or may not differ

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16
Q

Efficiently of translation

A

More efficient in prokaryotes because there is no nucleus, so there is no separation between transcription and translation

Multiple ribosomes can bind to one mRNA

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17
Q

Regulatory proteins

A

Found in major groove

Homodimeric

Structural motifs help bind to DNA:
Helix-turn-helix, Zinc finger, Leucine zipper

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18
Q

DNA Polymerase III in Arch. and Euk.

A

B=> replication

A&C=> repair

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19
Q

DNA Polymerase III in Prok.

A

A&B=> repair

C=> replication

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20
Q

DNA Polymerase III

A

Needs a primer

Goes 5’ to 3’

Proofreading capabilities

3’ to 5’ exonuclease activity

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21
Q

topoisomerase

A

Relieves supercoiling

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22
Q

primase

A

Lays down an RNA primer

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23
Q

Getting ready for DNA Polymerase at

Origin of Replication

A

DnaA binds

DnaB (helicase) binds: pulls apart double helix

Single-stranded binding proteins

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24
Q

Okazaki Fragments in Prok.

A

1000-2000 bases

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25
Q

Okazaki Fragments in Euk. and Arch.

A

100-200 bases

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26
Q

DNA Polymerase I

A

Removes RNA primers

Has 5’ to 3’ exonuclease activity

Add DNA

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27
Q

DNA Ligase

A

Connects DNA fragments together

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28
Q

Theta structure

A

What allows bacteria to divide so rapidly

DNA replication can start in many “layers”

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29
Q

Termination Site (Ter Site)

A

Tus protein binds and physically disrupts replication forks

Topoisomerase also involved

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30
Q

Tus protein

A

binds and disrupts replication forks

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31
Q

Arch. # of Origin of Replications

A

multiple

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32
Q

Prok. # of Origin of Replications

A

one

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33
Q

RNA differences to DNA

A

Contains Uracil instead of Thymine

Single stranded

Has ribose

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34
Q

Transcription

A

RNA polymerase

Promoters help RNA to bind

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35
Q

RNA Polymerase

A

5 subunits

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36
Q

σ factor

A

Recognizes the promoters exposed in major grooves

Leaves after recognition

Also involved in: endospore formation, different consensus sequences

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37
Q

Promoters

A

Always upstream of gene start site

Pribnow Box and -35 Sequence

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38
Q

Pribnow Box

A

Upstream 10 base pairs

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39
Q

-35 Sequence

A

TTGACA

Upstream 35 base pairs

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40
Q

TATA Box

A

Upstream 30 base pairs

Only Arch and Euk

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41
Q

RNA Polymerases in Arch.

A

Only one

Similar to Euk’s II

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42
Q

RNA Polymerases in Prok.

A

Only one

Not similar to any others

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43
Q

RNA Polymerases in Euk.

A

I, II, and III

II similar to Arch.

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44
Q

Intrinsic terminators

A

Based on mRNA structure

Hair-pin shaped loop

Inverted repeats

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45
Q

Hair-pin shaped loop

A

Immediately following gene is a stretch of U

Before that are sequences of a.a. in opposite order

Interacts with RNA polymerase and breaks

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46
Q

Rho-dependent transcription termination

A

RUT Site=> Rho Utilization Site

RNA polymerase pauses when it reaches loop

Rho protein then cleaves the strand

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47
Q

mRNA in Euk.

A

monocistronic

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48
Q

mRNA in Prok and Arch

A

polycistronic

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49
Q

Introns in Euk.

A

Do not lead to specific proteins

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50
Q

Introns in Prok.

A

NO INTRONS

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51
Q

Exons in Euk.

A

Lead to specific proteins

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52
Q

Ribonucleoproteins

snRNP’s

A

Remove introns in Euk.

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53
Q

5’ Cap in Euk.

7-methyulguanosine cap

A

Initiates translation procedure

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54
Q

Poly A tail in Euk.

A

At 3’ end

200 bases long

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55
Q

Poly A tail in Prok.

A

Means it’s targeted for degradation

10-40 bases long

56
Q

How many different codons?

A

64

57
Q

Wobble Site

A

Third spot in the codon

58
Q

Shine Dalgarno Sequence

A

16S rRNA finds this sequence at 5’ end before start codon and it complimentary base pairs with a.a. on 3’ end of 16S rRNA

59
Q

Amino-acyl tRNA Synthetase

A

Adds in amino acid

Located on 3’ end of tRNA

60
Q

tRNA

A

90 nucleotides long

folds make it more stable

61
Q

Large subunit of rRNA in Prok

A

50S

5S and 23S rRNA

62
Q

Small subunit of rRNA in Prok

A

30S

16S rRNA

63
Q

Prok. Ribosome

A

70S

64
Q

Euk. Ribosome

A

80S

65
Q

Large subunit of rRNA in Euk

A

60S

28S, 5.8S, and 5S rRNA

66
Q

Small subunit of rRNA in Euk

A

18S rRNA

67
Q

Formyl-Methionine

A

AUG Initiator Group

Attached first in prok

68
Q

Initiation of Protein Synthesis

A

30S subunit binds

Formyl-Methionine attached

Then, 50S subunit binds

69
Q

DNA designation for proteins Euk

A

3% of DNA

70
Q

DNA designation for proteins Yeast

A

70% of DNA

71
Q

DNA designation for proteins Bacteria

A

90% of DNA

72
Q

A T

A

2 H-bonds

73
Q

C G

A

3 H-bonds

74
Q

DNA A Form

A

11 bases per turn

75
Q

DNA B Form

A

10 bases per turn

76
Q

Histones

A

Euk and Arch

Supercoiling comes form wrapping around these

77
Q

DNA Gyrase

A

Negative supercoiling

Many antibiotics target this

78
Q

Reverse DNA Gyrase

A

Positive supercoiling in hyperthermophiles

79
Q

Adenylate cyclase presence of glucose

A

adenylate cyclase synthesis inhibited

cAMP transported out of the cell

80
Q

Missense mutation

A

1st or 2nd place in codon changed

81
Q

DnaK and DnaJ

A

ATP dependent

chaperones that allow for properly folded proteins

82
Q

Negative control of transcription

A

Occurs when the DNA binding protein (repressor) inhibits initiation of transcription

Operator DOWNSTREAM

Repression or Induction

83
Q

Adenylate cyclase absence of glucose

A

active

84
Q

Nonsense mutation

A

stop codon created

usually results in an incomplete protein

85
Q

GroEL and GroES

A

ATP dependent

for more stubborn proteins

only about 100 genes in E. coli need this

86
Q

Operator

A

Where the repressor protein binds

87
Q

Diauxic growth

A

Two phases of growth because changing of glucose to lactose

lag phase in between

88
Q

Silent mutation

A

3rd or Wobble site changed

results in a normal protein

89
Q

Constitutive proteins

A

always expressed

“housekeeping genes”

90
Q

Repression

A

Anabolic pathway

91
Q

Attenuation

A

Occurs DURING transcription

Only in Prok.

92
Q

Feedback inhibition

A

Post-translational control

typically targets first enzyme

93
Q

Induction

A

Catabolic pathway

94
Q

Tryptophan plentiful

A

The ribosome will continue translation

Subunits 3 and 4 of mRNA will bind

RNA polymerase terminates and genes aren’t transcribed

95
Q

Allosteric site

A

Once bound, the conformational changes prevents the binding of substrate

96
Q

Arginine operon

A

REPRESSION (NEGATIVE CONTROL)

Excess Arginine acts as a corepressor and binds to the repressor to block RNA polymerase which blocks transcription

97
Q

Tryptophan scarce

A

The ribosome will stall

Subunits 2 and 3 of mRNA will bind

RNA polymerase continues to transcribe genes

98
Q

EF-Tu

A

Helps load tRNA’s into the A site

Active when bound to GTP

99
Q

Concerted feedback inhibition

isoenzymes

A

different enzymes that catalyze the same reaction but are under different regulatory control

100
Q

The Lac Operon

A

INDUCTION (NEGATIVE CONTROL)

Repressor binds when lactose is absent. When lactose is present, it acts as an inducer and binds repressor thus allowing transcription to proceed

101
Q

Sensor kinase protein

A

Found in cytoplasmic membrane

typically autophosphorylates at the histidine residue

Ex) EnvZ

102
Q

EF-Ts

A

Catalyzes the binding of GTP

Reactivates EF-Tu

103
Q

Covalent modification of enzymes

A

AMP used to modify enzyme

Can also add ADP, PO4, CH3

104
Q

Difference between Positive and Negative Transcriptional control

A

The binding location

Positive=> UPSTREAM

Negative=> DOWNSTREAM

105
Q

Response regulator protein

A

phosphate transferred to response regulatory protein

cytoplasmic DNA binding protein

Ex) OmpR

106
Q

Base analog

A

Is mistakenly integrated into the genome

107
Q

Example of a chemical mutating DNA

A

ethidium bromide

108
Q

Rec A protein

A

SOS Response

binds and holds gaps together

109
Q

Sfi A Protein

A

SOS Response

inhibits cell division

110
Q

DNA Polymerase IV and V

A

Used in SOS Response

111
Q

carcinogenic

A

causes mutations

112
Q

Bruce Ames

A

developed Ames Test in 1970’s

113
Q

Mutational reversion assay

A

Salmonella typhimurium used (Histidine auxotrophs)

cell wall altered so it’s more penetrable by chemicals

repair mechanisms removed

114
Q

Ames Test

A

Control Plate: Bacteria, molten agar with small amount of Histidine

Test Plate: Bacteria molten agar with small amount of Histidine, chemical to test mutagenicity

115
Q

Auxotroph

A

only grows on a medium that provides a lacking amino acid or nucleotide

116
Q

Morphological mutations

A

changes that can be seen

117
Q

Lethal mutations

A

cannot survive

118
Q

Conditional mutations

A

only seen under certain environmental conditions

119
Q

Biochemical mutations

A

a biosynthetic pathway inactivated to change the biochemistry of the cell

interrupt an amino acid or nucleotide

120
Q

Frameshift mutation

A

occurs when base pairs are deleted or inserted

alters the reading frame

121
Q

Reversion mutation

A

when an earlier mutation is reversed by a second mutation

122
Q

Same-site (true) reversion

A

converts the mutant nucleotide sequence back to the original sequence

123
Q

Second-site reversion

A

a second mutation occurs at a different site in the DNA and causes the wild type phenotype to be restored

124
Q

Induced mutations

A

results from exposure to known mutagens which are primarily physical or chemical agents that interact with DNA in a disruptive manner

125
Q

Spontaneous mutations

A

a random change in the DNA arising from errors in replication

126
Q

Ethidium bromide

A

an example of an induced mutation producing chemical

127
Q

Ionizing radiation

A

radiation ejects orbital electrons from an atom and causes ions to form DNA BREAKAGES

Gamma rays (most penetrating)

Cathode rays (least penetrating)

128
Q

Nonionizing radiation

A

Radiation that excites an atom to a higher energy state

UV radiation

absorbed by DNA and creates pyrmidine (CT) abnormal bonds in DNA

129
Q

Ultraviolet light

A

only targets the surface

130
Q

Nucleotide Excision

A

Involves UVR-ABC enzyme

removes distortion, usually 12 nucleotides

DNA Polymerase I fills in gaps

DNA Ligase fuses them back together

131
Q

Excision Repair

A

Corrections to distortions in DNA

132
Q

SOS Response

A

Works to repair problems in the absence of a template strand

ERROR PRONE LAST DITCH EFFORT

133
Q

Base Excision

A

DNA Glycolsylase severs bonds between the two bases

AP endonucleases nick DNA

DNA Polymerase I removes and replaces base

134
Q

Direct Repair Mechanism

A

Photoactivation

thymine dimers caused by non-ionizing radiation removed with photolyase

135
Q

Photolyase

A

removes Thymine dimers caused by non-ionizing radiation

136
Q

DNA Glycolsylase

A

severs bond between two bases during Base Excision

137
Q

AP endonucleases

A

nick DNA during Base Excision