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Lecture 14: Gene Expression Pt. 2

Today:

  • Methods of measuring gene expression experimentally
  • How to write an equation for gene expression
    • Use the central dogma!
    • Fill in the parameters with the measurements we examined last lecture
  • An example of a simple use of the model

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Our starting point: the central dogma of biology

DNA

gene

DNA

RNA

protein

transcription

translation

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Gene expression in bacteria

promoter

protein coding sequence

gene

RNA polym.

repressor

activator

some

ribo

protein

mRNAs can be destroyed

proteins can be destroyed

Transcription can be repressed by a protein

Transcription can be activated by a protein

Can respond to environment.

mRNA

Goal: use this framework to build toward equations that will let us:

  • Understand the dynamics of each component of gene expression
  • Analyze genes that regulate each other

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Our basic framework

DNA

mRNA

protein

For a given gene:

Let [m] by the concentration of the mRNA for the gene and [P] be the concentration of the protein.

How to we describe the dynamics of these molecules within the cell?

 

 

transcription of DNA into RNA

active degradation of mRNA, dilution due to growth

translation of mRNA into protein

active degradation of protein, dilution due to growth

Can be influenced by the level of another gene or itself through gene regulation!

[m]

[P]

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What do we need to build and test a model?

We need to know several rates to set parameter values in our equations

  • What are the rates of mRNA production from DNA?
  • What are the rates of mRNA loss?
  • What are the rates of protein production from mRNAs?
  • What are the rates of protein loss?

Then we need to know

  • How do we incorporate those rates into the equations?
  • How do we represent gene regulation mathematically?

How do we measure gene expression in cells to compare to models?

Last time!

Today!

Next week!

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How is mRNA “lost”? What are the rates of loss?

Ribonuclease (RNase) enzymes actively degrade RNAs.

mRNA

RNase

+

How quickly does this happen to an mRNA in a cell?

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What are the half lives of mRNAs?

Very short! Most genes degraded to half their concentration in less than 6 minutes!

Interesting note from these authors: no correlation observed between mRNA half life and 1) abundance, 2) secondary structure, or 3) cell growth rate.

Note: these half lives reflect much faster degradation than would be accounted for by dilution due to cell growth.

Active degradation is the dominant factor for mRNA loss!

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How is protein “lost”? What are the rates of loss?

Measured rate of radioactivity of perfusate

Fast component of protein degradation

Slow component of protein degradation

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How is protein “lost”? What are the rates of loss?

fast

slow

They are able to estimate two things:

  1. The half-life of the fast component
  2. The percentage of total protein the

Findings:

  • Average half-life for fast component is ~60 minutes
  • Fast component accounts for 5-7% of total protein
    • Under some conditions as low as 2%!

Conclusion: active, rapid degradation is not a major component of protein loss in E. coli.

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To summarize

DNA

mRNA

protein

Similar synthesis rates

Loss is fast; mainly due to active degradation by RNases

Loss is slow; mainly due to dilution from growth

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What we found last lecture

DNA

mRNA

protein

active degradation

transcription

translation

dilution due to cell growth

active degradation

dilution due to cell growth

 

 

Thinking about concentrations in the cell:

similar rates

dominant factor

dominant factor

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What will these measurements tell us?

DNA

mRNA

protein

transcription

translation

 

 

Depending on regulation, this will predict:

  • How protein level responds to changes in mRNA level
  • The dynamics of gene regulation
    • A gene the regulates itself
    • Genes that regulate other genes

In order to test these predictions, we have to measure gene expression. How do we do that?

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Measuring gene expression

DNA

mRNA

protein

transcription

translation

  • Can be measured at the level of mRNA or protein
  • Can be population-level or single-cell-level�
  • Can be time resolved or a “snapshot” at a particular time

vs.

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Measuring bacterial gene expression with fluorescent proteins

gene of interest: tapA

tasA

protein coding sequence

PtapA

6. Method 1: transcriptional reporters, transcription-level

promoter

gfp

PtapA

Create a mutant with the following sequence elsewhere in the genome:

Same regulatory sequence. gfp is regulated the same way as tasA in this cell. If you seen no GFP signal in a cell, it’s probably not making a lot of tasA. If you see a lot of signal, it’s probably making a lot.

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Measuring bacterial gene expression with fluorescent proteins

1. Method 1: transcriptional reporters

PcitZ-YFP

(B. subtilis)

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Measuring bacterial gene expression with fluorescent proteins

gene of interest: tasA

gfp

tasA

protein coding sequence

PtasA

6. Method 2: fluorescent protein fusion, protein-level

Create a mutant with:

The protein is made with a fluorescent protein physically connected.

Only used when spatial protein localization is strictly needed because attaching GFP changes a protein’s behavior in unknown ways!

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Method

Molecule(s) measured

Pros

Cons

Western blot

Protein

  • Still gold standard for detecting a protein
  • Very labor-intensive
  • Need antibodies
  • No spatial or temporal information

RNA sequencing

RNA

  • Many genes
  • Single-cell or nearly single-cell information
  • No time information
  • Data can be hard to interpret

Proteomics w/mass spec

Protein

  • Many/all genes
  • No time/space
  • Need fancy instrument

RNA FISH

RNA

  • Spatial information
  • Potentially many genes at once
  • Expensive/difficult
  • No time information

Transcriptional fluorescent protein reporters

RNA-ish

  • Time dynamics (some)
  • Single-cell reporting
  • # genes limited by spectral overlap
  • Time dynamics confounded by separation of time scales between mRNA and protein processing

Fusion fluorescent protein reporters

Protein

  • Single-cell-level
  • Time dynamics
  • Spatial protein reporting
  • Attaching a fluorescent protein to gene of interest alters its properties
  • Difficult/impossible to make for, e.g., membrane proteins
  • # genes (see above)

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Now back to our model

DNA

mRNA

protein

active degradation

dilution due to cell growth

active degradation

dilution due to cell growth

 

 

How do we turn this

into terms for these equations?

First, we’ll look at the case of unregulated or “constitutive” gene expression: mRNA is always being made.

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How do we write the terms of our equation?

First, note that we’ll measure concentration in units of molecules per cell.

Remember from the first lecture, 1 molecule per cell is ~1 nM.

 

What is the rate of mRNA production?

Units of

concentration

time

molecule/cell

time

=

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mRNA production

From last lecture:

gene

~1000 nt

RNAp

mRNA

~16.17 sec

So a single RNA polymerase produces ~1 mRNA in 16.17 seconds, or a rate of

 

But a single gene can fit ~18 polymerases (55 nt footprint), so the maximum rate is then

 

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How do we write the terms of our equation?

 

What is the rate of mRNA loss?

We saw last lecture that active mRNA degradation results in a half-life of ~5 minutes. What does this mean?

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How to write out the mRNA degradation term

We saw last lecture that in a variety of conditions, mRNAs are degraded with a half-life of ~6 minutes in the absence of transcription.

This corresponds to our equation with a transcription rate of 0:

 

0

A 6-minutes half life means that every 6 minutes, the concentration of mRNA is divided by 2.

The mRNAs are decaying exponentially! What’s the equation for that?

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Exponential decay of mRNAs without transcription

 

0

 

 

 

We now have an equation for the concentration of mRNA in time.

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Equation for constitutive mRNA production

 

 

 

 

We considered the situation where the mRNA had the maximum number of polymerases on it. In reality no promoter binds polymerase well enough for this to be true. A real value will be much lower.

What about protein??

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Protein production for this gene

 

What is the rate of protein production?

Units of

concentration

time

molecule/cell

time

=

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Protein production

From last lecture:

mRNA

~1000 nt

ribosome

protein

~16 amino acid / sec

333 codons per mRNA

A single ribosome produces ~1 protein in 21 seconds from an mRNA, or a rate of

 

But a single mRNA can fit ~28 ribosomes (35 nt footprint), so the maximum rate is then

 

 

But there are also [m] mRNAs in the cell and this is per mRNA! The production term is:

 

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What about protein loss?

We saw that for 95% of proteins, active degradation is extremely slow. The major contributor to loss of protein concentration is dilution due to cell growth.

In that case, the half-life for a protein is just the cell doubling time. If the cell volume doubles in one doubling time, then the protein concentration will be reduced by a factor of 1/2 because concentration is inversely proportional to volume. In that case the loss term is:

 

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Our protein equation:

 

 

Translation from mRNA

Dilution from cell growth

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Equations for the production of a constitutively expressed gene

 

 

 

 

 

 

We can now solve this system of equations in python to look at the dynamics of mRNA and proteins in the cell. What does this look like for a 60-minute doubling time?

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Let’s start Jupyter

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Our solution:

Due to fast degradation, mRNA reaches a maximum level very quickly!

mRNA production perfectly canceled by mRNA degradation

Due to much slower degradation, protein takes a long time to reach a maximum level!

Concept of “separation of time scales

Notice both of these y-axes is larger than the values we saw measured in lecture 2.

This is because we assumed the maximum possible transcription rate. Not true for any real gene!

(Started from an unrealistic condition of no mRNA or protein)

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Hypothetical scenario

We saw in our previous example that once an mRNA started being produced, the protein for the gene took ~10 hours to reach a steady-state level.

What if at 10 hours a repressor starts being produced that prevents transcription?

protein coding sequence

promoter

DNA

What happens to the protein and mRNA levels?

repressor

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How do we use our model for this hypothetical?

The initial condition was:

 

Our equations from the central dogma were:

 

 

We solved them to get the concentration of mRNA and protein after 10 hours.

Now a repressor binds and transcription goes to 0!:

 

 

0

 

 

Now solve these equations with the initial condition being our first solution at 10 hours:

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Repression after 10 hours

The cell senses something and makes a repressor. What happens?

Happily making the gene

???

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Repression after 10 hours

The cell senses something and makes a repressor. What happens?

Happily making the gene

mRNA decays very quickly!

Protein sticks around for a while

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What have we learned?

  • You can measure gene expression at the mRNA level or protein level, in time or with a snapshot, at the population level or single-cell level
  • Using the central dogma and measured production, degradation, and dilution rates, you can write equations to describe the concentration of a gene in a cell
  • This model can predict response time scales�

Next:

  • How do we incorporate regulation into this model?
  • Given the infinite number of possible gene regulatory networks, how do we figure out which networks are important?