Exam 2 Gene Expression/Western Blot
Why do we want gDNA?
want to study the Promoter region
gDNA has all the necessary noncoding and going regions i.e. exon and introns
Gene Expression Analysis:
Northern Blot
RT-qPCR
~~RT-qPCR
produce more PD2 (proliferated) and DD7 (differentiated)
~SYBR Green Supermix (2x rxn)
Amplify
Taq Polymerase (antibody-mediated)
Buffer
DNTPs
MaCl2
RT rxn (template)
Primers (forward and reverse)
Quantity
SYBR Green (fluorescent)
Enhancer and Stabilizer
ROX passive dye
SYBR Green
will bind to dsDNA causing fluorescents
Taq Polymerase (antibody-mediated)
prevents Taq from binding till needed
the antibody will denature till 95C
the antibody binds to protein to prevent rxn from occurring
ROX passive dye
baseline Ct reading will not change
Enhancer and Silencer
transcription factors that bind to sequences in the promoter region
TAA derivatives
prevent primers from associating to SYBR Green
Cross Ct- line (cycle threshold)
the sooner the Ct-line is passed the more inial RNA we have
gene expression is higher
the longer it takes to pass the Ct-line the lesser inial RNA we have
gene expression is lower
Platue
All SYBR Green is bound
Melt curve
The longer it takes, the longer the amplicon
The shorter it takes, the shorter the amplicon
two peaks for one, possible contamination
Two peaks from two means one is short one is long, better.
~~Primers
18 - 22 bp
75 - 150bp (amplicon)
GC content (40% - 60%)
both GC have to be around the same content
Cross Exon Exon junction
Primers need to avoid gDNA contamination to eliminate the impact
Exon Exon junction
keeps a Short amplicon,
lowers the chance of contamination
end with AG - that is what the spliceosome recognizes
AG/ GU rule
Cuts end then covalently lariad structure that it releases
*Can put primers on certain exons to distinguish between multiple possible spice variants going on.
Alternative Splicing:
Primers can be placed on certain exons to distinguish between multiple possible splicing variants
~~DNA isolation (RT-qPCR)
GAPDH
reference gene
GAPDH gene and Gene of interest should be the same or close numerically when measured
The reference gene is used to correct for variation in biological replicates if something went wrong with RNA preps.
Reference genes tell us if variation in biological replicates is because of something normal for that gene or because of something that went wrong with the RNA preps. If the biological replicates and reference genes go up the same way, then it means the RNA preps were not good.
~~Promoter Region
used to study how a gene is regulated
RT-qPCR can not do this
~Isolate Promoter: (PCR)
-promoter DNA is gDNA that has the sequence we will PCR amplify
Purify gDNA
(Look in the database for sequence)
Create primers
PCR
Use primers to amplify fragments of the promoter of interest based on the promoter sequence
Engineer restriction digest (identify where plasmids go)
Insert into a reporter plasmid
How to clone promoter region?
PCR
Process:
Purify PCR product
Digest
Ligate into reporter plasmid
Transformation and inoculate
Mini - prep
Run gel
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Reporters do not come w/ promoters
Need to design primers to PCR amplify
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Review
PCR amplify fragments of the gene promoter
What enzymes do we need to cut?
Restriction digest
Forward primer and reverse primer
needed to amplify both strains of dsDNA
Marks the region you want to amplify
~Reverse primer binds to the template (near the first Exon)
~Forward primer binds to the complementary
Why multiple fragment sizes?
We do not know what is in the sequence in the regulatory regions
What is the problem of taking the regulatory region from one gene and ligating to another gene?
There is always the possibility of missing a regulatory element
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The regulatory region
PSEAP-2
Reporter plasmid
Amplify Reporter plasmid w/ PCR
Analyze sequence -UBR 5
Design Primes
GC content
length
*Do not cut DNA within in sequence. hjhjbjhbjh
*Recognize the sequence of plasmid we want to clone into reporter.
Transfect into cells
NEB cutter sequence
mlu 1
Cutter Sequence needs to be in the MCS
PCR -digest
Analysis
transfect
Trasfect - introduce recombination gene into the cell, gene will activate transcription
The reporter gene should transcribe
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Restriction digest analysis:
Multi fragment sizes
differences in the fragment sizes narrow where regulatory elements exist
look at enzymes,
cut reporter plasmids MCS,
cut primers,
should not cut gDNA
Get recombinant plasmid: (look at chart)
Trasfect into cells
Introduce DNA into Euk cells
Recomb gene transcriptionally active
The reporter gene should be transcriptionally active
Cells make a lot of SEAP protein in growth media
SEAP protein (if transfected will transcribe causing light)
transfect
media
Add SEAP substrate (heat up to 65C to denature phosphatase)
Produce light
measure amount of light (RLU)
Enhancers:
Elements unique to the promoter that cause it to be responsive to the same conditions.
Canonical
response element sequence
MRFs (myogenic regulatory factors)
Myogenin
MyoD
Proteins that regulate transcription
Only capable of binding DNA to response element with certain seq of nucleotides
Bind to the enhancer sequence called E-box.
E-box location in the promoter
5` CAN N TG `3
Genes w/ E-box can respond to MRFs and expression
Clone fragment into receptor Plasmind:
Run SEAP
Identify potential E-box sequence
What do we expect the promoter to do?
MRF should drive RLU higher if you have MRF present along with the reporter gene.
Site-directed Mutagenesis: (look at charts)
Reporter plasmid with SEAP gene and promoter with E-box
Forward Primer
Spans across E-box, change
Change 2 nucleotides in the primer
(Everything else is the same as a primer will bind.)
Reverse Primer
The exact same complementary sequence
Primers become part of PCR product
~Find template Plasmid vs. PCR amplified Plasmind?
Template Plasmid was grown in the presence of bacterial cells
Bacteria methylates DNA in certain places.
Use Enzymes Dpn1 to digest rxn afterward
only recognizes 4bp sequence that has to be Methylated
Cuts only the template DNA into fragments
PCR product DNA is left behind
How do you find the Plasmids that you want in a mixture?
Transformation
Bacteria takes up mutagenic plasmid
**Western Blot**
~~ ULB +
Lysosomes have lots of proteases. We want to protect proteins as we lyse cells.
Lysosomes will not work when pH around 5.
Protease Inhibitors 2. Phosphatase inhibitors
1. Protease Inhibitors: Cocktail
Aptoninin: Serine protease inhibitor
Chymastatine: Serine and Cysteine protease inhibitor
Leupeptin: Serine and Cysteine protease inhibitor
Pepstain: general Inhibitor (blocks lots of Proteases)
2. Phosphatase inhibitors: Cell signaling
Beta- glycerophotase *
Sodium molybdate *
Sodium othoranadate *
*main ones*
DMSF
3. DTT : Breaks disulfide bridges
Make ULB (Lysis Buffer)
SDS
Tris
NaCl
NaF pH inhibitor
DTT
Do 5’ fold and 10’ fold dilutions with lysis buffer and do reading of those
whichever one gives you reading within the linear range of the assay is one you’ll use.
*Western Blot*
RNA —→ Protein
Translation —> Western Blot
Isolate Protein from tissue or cells
Lyse cells — make homogenate
Basis* ULB
Lysis Buffer (ULB):
1. Detergent: (SDS) non-ionic detergent*
NP-40
Triton X100
5% w/v
2. Tris: pH regulator*
pH 7.5
50 mM
3. NaCl (salt) - 50 mM*
Dissolves into ionic form when mixed with H2O
Change the salinity of the solution around the cell
create hypotonic solution
lots of ions inside cells
Water rushes in, destabilizing the membrane
Lyses cell
4. NaF: Phosphate inhibitor - 50mM
Make Buffer
Weight out solids
Add water (amt. based on solvent)
Add HCl to bring pH down to 7.5
Add water
Protein Assay:
Protein Assay: Bradford Assay
Commassile Brilliant blue G - 250 dye
Dye binds to basic amino acids arginine and aromatic a.a
changes to blue
More protein you have, more dye that binds, more blue you get
If we do lysis and have concentrated protein lysate we’ll have to serail dilute a couple of times.
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y=mx+b x is mult by 2 or 5.
look at notes for math portion
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SDS-Page: (gel electrophoresed for proteins)
Sodium dodecyl sulfate Polyacrylamide gel electrophoresis (8% -12%)
anionic detergent
Coats proteins
uniform negate charge
Acrylamide
thin, run up and down, separate proteins.
Glycine
an amino acid that can be protonated or deprotonated
TEMED
the catalyst causes the cross-pattern
APS
catalyst polymerizes acrylamide
Loading dye for SDS-PAGE
Mix diluted proteins with loading dye
Tris Buffer -7.5
Bromophenol Blue
Glycerol
DTT
Glycine
Gel components: what do they do?
Tris pH 6.8 standing
Tris ph 8.8 running
Glycine
SDS
Acrylamide
Bis - acrylamide
APS
TEMED
H2O
Running buffer
SDS
Glycine
Tris
Shape- linear
denature 95C for 5 min
Breaks disulfide bridges (DTT or Beta- mercaptoethanol)
Reducing agents
~~Transfer
Buffer
Glycine
Tris
Structure for gel stain
Metal plate
filter paper
PVDF membrane (methanol)
Gel
Filter paper
Metal plate
PVDF has the transfer
Stain membrane with
Ponceau S (red dye)
protein adhesión
Wash H2O
Block with milk in T-TBS
Clean off any weakly associated bonds
Saline weak ion and bonding
weak hydrophobic
Process:
Milk - fill all open spaces on the membrane
Wash T-TBS
3x -5min
Incubate with 1` antibody diluted with MyHC
in 5% milk + T-TBS (10mL)
1-2hr @RT
Wash T-TBS
3x -5min
Incubate with 2` antibody
5% milk + T-TBS (30-60 min)
Wash T-TBS
3x -5min
Develop
light production
What is the purpose of using a secondary antibody for western blotting?
Bind to the primary antibody, Amplify the level of the detection signal, and Eliminate the need to enzyme-conjugate every primary antibody.