RNA and Protein Flashcards

1
Q

Kinds of RNA

A
  • messenger RNA
  • transfer RNA
  • ribosomal RNA
  • catalytic RNA
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2
Q

mRNA

A
  • template for protein synthesis
  • contains the message (coding region) that is translated by the ribosome into protein, as well as some untranslated RNA involved in ribosome recognition and termination
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3
Q

tRNA

A
  • decodes the message and loads the amino acid
  • contains antidon complementary to codon
  • charged with AA corresponding to anticodon
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4
Q

rRNA

A
  • together with the ribosomal proteins make up the ribosome
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5
Q

catalytic RNA

A
  • RNA enzymes involved in diverse processes.
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6
Q

RNA base pairs

A
  • takes on the form of stem loops
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7
Q

greatest to least prevalence of RNA in cell

A

rRNA>tRNA>mRNA

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8
Q

RNA synthesis - transcription

A
  • transcribed from DNA via a DNA-dependent RNA polymerase
  • synthesizes RNA 5’ -> 3’
  • RNA is transcribed from DNA
  • RNA pol does not require a primer
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9
Q

RNA pol binds to which strand

A
  • template strand
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10
Q

RNA produced has the same sequence as the

A
  • coding strand
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11
Q

3 steps of transcription

A
  • initiation - RNA pol binds to promotor
  • elongation - RNA is polymerized
  • termination - RNA polymerase detaches
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12
Q

RNA polymerase subunits

A
  • alpha - chain initiation and interaction with regulatory protein
  • beta - DNA binding and RNA elongation
  • beta prime - DNA binding subunit
  • sigma - promotor recognition
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13
Q

why multiple sigma factors

A
  • each is used for different growth conditions and recognizes slightly different promotors.
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14
Q

holoenzyme

A

all 4 subunits together

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15
Q

core enzyme

A

consists of only a, b, and b’

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16
Q

promotor structure

A
  • transcription initiated here. promotor not transcribed
  • binding site for polymerase
  • conserved sequences at -10 and -35
  • transcription start site is +1
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17
Q

Pre-initiation

A

binding of sigma factor to RNA polymerase core converting polymerase to holoenzyme

18
Q

Pol binding

A
  • binding of holoenzyme (open hand) to promotor DNA sequence

- wrapped of DNA around holoenzyme (touches about 75-80 bp)

19
Q

formation of open complex

A
  • closing of open hand structure
  • melting of about 10-15 bases
  • incorporation of monomers into polymer until a length of about 10
20
Q

elongation

A
  • holoenzyme loses sigma factor and loses contact with -10 and -35 regions of promotor
  • the core contacts 30-40 DNA bases and can incorporate 30-60 RNA monomers/sec
21
Q

termination

A
  • elongation stops
  • transcript RNA is released
  • dissociation from DNA
22
Q

two main classes of termination

A
  • rho dependent
  • rho independent
  • both rely on formation of stem loop (inverted repeats)
23
Q

rho independent termination

A
  • RNA stem loop causes the polymerase to stall

- poly-U stretch behind the stem doesn’t have enough energy to hold RNA-DNA hybrid together and complex falls apart

24
Q

rho dependent termination

A
  • Rho assembles as a hexamer on G-C rich RUTS on RNA. Stem loop forms
  • translocates up RNA, catches up to RNAP, and dissociates RNA-DNA hybrid through helices activity.
25
Q

RNA stability

A
  • rRNA and tRNA stable due to large amounts of secondary structure
  • mRNA is not stable
26
Q

post-translational processing of protein

A
  • cleavage
  • insertion of non-protein ligands
  • chaperon-mediated folding
  • association with other proteins
27
Q

protein primary structure

A
  • sequence of amino acids
28
Q

protein secondary structure

A
  • alpha helix
  • beta sheet
  • fold due to R groups on primary sequence
29
Q

protein tertiary structure

A
  • how helices and sheets interact + co-factors
30
Q

protein quartenary structure

A
  • interaction of two or more polypeptides
31
Q

protein folding

A
  • all information required for proper folding of a protein resides in its primary sequence
  • each protein has a thermodynamically defined stable structure
32
Q

mis-foldings

A
  • proteins often will not find the true thermodynamically favored structure without falling into “local” energy minima
33
Q

chaperones

A
  • help proteins fold
34
Q

ways chaperones help fold

A
  • proline peptidyl isomerase
  • binding/release of hydrophobic regions of protein
  • providing a safe surface/chamber for folding
  • providing energy to escape a local minimum
35
Q

GroEL

A
  • provides a safe surface for protein to fold if it falls into a local min
36
Q

GroES

A
  • provides the energy
37
Q

why proline needs it’s on chaperone protein

A
  • free rotation around all peptide bonds except protein

- PPI breaks bonds to allow for isomerization then reforms

38
Q

integral membrane protein

A
  • spans membrane many times

- inserted into membrane while being translated

39
Q

secreted proteins

A

proteins targeted for secretion have a hydrophobic signal sequence which directs them to the sec secretion apparatus

40
Q

sec system

A
  • most proteins use
  • proteins are secreted off the ribosome in a linear fashion before any folding as taken place.
  • fold in the periplasm
  • have signal sequence that contains charged residues following by a series of hydrophobic residues.
41
Q

tat system

A
  • can’t fold in periplasm
  • fold on inside then go outside
  • signal sequence that is recognized by two consecutive arginine residues located near N-terminus of protein
42
Q

open reading frame

A
  • the coding region of DNA and RNA