The gene is the protein coding sequence which means it is the section of DNA which is transcribed into mRNA to then be translated into the desired protein.

This gene comes from the coral Acropora millepora which is found in the Indo-Pacific coral reefs. You can find more information on Acropora millepora here.

The protein produced has a maximum absorbance of light at 588nm making it appear blue/purple to the naked eye. Genes like this that are visible to the naked eye tend to be used either to test to see whether a promoter works as expected or in combination with a promoter that’s known to work in order to detect changes in the environment that are known to activate the promoter.

Heat shock proteins (HSP) are a family of proteins produced by cells in response to stressful conditions and are found in almost all living organism, including humans. They’re call “heat shock” proteins because they were originally believed to only be produced when the cells suffered heat shock, meaning they’re exposed to temperatures above their ideal temperatures. It’s since been found that they can be produced by cells under other stresses such as cold, exposure to UV light and while healing tissue.

misfolded proteins

HSPs are generally molecular chaperones; this means they stabilize newly formed proteins to prevent them from becoming denatured ensure correct protein folding or help to refold proteins that have already been damaged by the cell stress as shown above. There are many types of HSP and they have different families named after their molecular weight; for example, Hsp60 and Hsp90 refer to two families of HSP of the order of 60kilodaltons and 90kilodaltons respectively.

HSPs are known to play a role in the cardiovascular system; Hsp90 binds to endothelial nitric oxide synthase and soluble guanylate cyclase which are both involved in vascular relaxation and HSP20 is known to prevent platlet aggregation (the clumping together of platelets which leads to the formation of clots). HSPs are also involved in the immune system as they can bind antigens. You can learn more about how HSPs are involved in the immune system here.

There’s research involved in using HSPs for cancer treatment and vaccination. Given their role in binding antigens to present to the immune system, they can be used to boost the effectiveness of vaccines, including those for cancer. Also, intracellular HSPs such as Hsp90 are crucial for the survival and cancerous cells so HSP inhibitors such as Tanespimycin could be potential solutions to many forms of cancer and is currently in clinical trials. You can learn more about the involvement of HSP’s in cancer here.

Pepsinogen is a zymogen, also known as a proenzyme. This means it’s an inactive precursor to an enzyme and will become the active enzyme when the active site is revealed after a biochemical change. In this case, pepsinogen will become pepsin (an enzyme involved in digestion) after being exposed to either HCl or pepsin. In the human body pepsinogen is released into the stomach.


Pepsin has many industrial uses such as food manufacturing, removing hair for leather production and recovering silver from old photographic films. Pepsin is also used for fragment antigen-binding. This is where an antigen is digested in order to separate the antigen binding portion of an antigen from the rest of it. The antigen binding portion produced by pepsin is known as F(ab’)2. It’s common to use these antibody fragments in investigations in which the Fc region (the section that’s removed) can interfere; for example, parts of the body such as lymph nodes and the spleen have Fc receptors which can interact with the Fc region. You can learn more about anitbody fragmentation here.

antibody digestion

This gene comes from the coral Discosoma striata, a genus of soft coral commonly known as mushroom coral native to the Indian ocean.

rfp coral
The protein causes the bacteria to appear red under normal light and pink under UV light. This happens because UV light excites electrons in the protein. The electrons then must return to their ground state and it does this in multiple steps emitting photons at each step, one of which is within the visible spectrum. You can learn more about fluorescence here.

The gene has an added degradation tag which means that the protein starts to break down almost immediately after being produced; this reduces the overall fluorescence as the protein doesn’t accumulate. This does, however, allow for greater temporal resolution of the red fluorescence, meaning that if the promoter is switched on and then off later the fluorescence is lost.. This is different to the blue chromoprotein which would keep it’s blue colour after the promoter is switched off.