The evolutionary capacitor

Image from LiveScience. Credit: Richard Borowsky Image from LiveScience. Credit: Richard Borowsky

Heat shock protein 90 (HSP90) helps keep proteins in the body folded properly and is thought to compensate for variations that occur in proteins over time. In a study published in Science magazine, Dr. Nicolas Rohner and colleagues showed that stress can affect the ability for HSP90 to do its job thereby unmasking these alternative versions of proteins which may lead to adaptation in some cases.

The theory was tested in fish called Mexican tetra (above), some of which adapted to life in caves leading to eventual loss of, or diminished, eyesight. The team of researchers blocked HSP90 in a group of surface dwelling fish and found that the fish developed wide variations in the size of their eyes and eye-sockets.  Exposing surface dwelling fish to water similar to that found in caves also caused the variations in eyes to develop. These findings led the researchers to hypothesize that HSP90 may be an "evolutionary capacitor" that helped the fish adapt to life in caves.

Source:

N Rohner, DF Jarosz, JE Kowalko, M Yoshizawa, WR Jeffery, RL Borowsky, S Lindquist, CJ Tabin. Cryptic Variation in Morphological Evolution: HSP90 as a Capacitor for Loss of Eyes in Cavefish. Science  1372-1375, 2013.

 

 

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By Managed Servic… (not verified) on 06 Apr 2014 #permalink

Proteins play an important role in the cells of living organisms and are composed of 5 elements which living cells consist of - Carbon, Hydrogen, Oxygen, Nitrogen, Phosphor and Sulfur. All of these elements come forth in different types of proteins which has functions such as : Transport proteins, support proteins, enzymes, hormones, monement in muscles done by kinesin and myosin, ect. One type of protein which assures that proteins keep their functional original shape is chaperone proteins. When denaturation ( disformation of roteins ) occurs, chaperone proteins absorb the denatured proteins and remature them (transforms / reshapes (rematures) them back to their original functional shape). ATP is oxidised to ADP+P during this process and the process occurs to assure that properly functional proteins comes forth in the body. Heat shock protein is one type of chaperone protein which refolds proteins which has denatured because of excessive temperatudes such as extreme hot or cold. It gives cells the ability to survive in extreme temperatures for a certain amount of time and gives them the ability to return to their original proper function after they were temporarily damaged because of the extreme temperatures(adapt). When chaperone proteins do not come forth in the cells of an organism, this could result in mutations which brings forth changes and differences in the cells of an organism. It could also lead to starvation of the organism because of a disability to reform dematured(misformed) proteins. an example of denaturation of a protein is an egg hardening and changing color when cookedn(extreme temperature-heat) -chaperone proteins are unable to adapt and reshape proteins in time.
Thus, proteins such as chaperone proteins play an importaint role in

By David van der … (not verified) on 23 Apr 2014 #permalink

Proteins play an important role in the cells of living organisms and are composed of 5 elements which living cells consist of – Carbon, Hydrogen, Oxygen, Nitrogen, Phosphor and Sulfur. All of these elements come forth in different types of proteins which has functions such as : Transport proteins, support proteins, enzymes, hormones, monement in muscles done by kinesin and myosin, ect. One type of protein which assures that proteins keep their functional original shape is chaperone proteins. When denaturation ( disformation of roteins ) occurs, chaperone proteins absorb the denatured proteins and remature them (transforms / reshapes (rematures) them back to their original functional shape). ATP is oxidised to ADP+P during this process and the process occurs to assure that properly functional proteins comes forth in the body. Heat shock protein is one type of chaperone protein which refolds proteins which has denatured because of excessive temperatudes such as extreme hot or cold. It gives cells the ability to survive in extreme temperatures for a certain amount of time and gives them the ability to return to their original proper function after they were temporarily damaged because of the extreme temperatures(adapt). When chaperone proteins do not come forth in the cells of an organism, this could result in mutations which brings forth changes and differences in the cells of an organism. It could also lead to starvation of the organism because of a disability to reform dematured(misformed) proteins. an example of denaturation of a protein is an egg hardening and changing color when cookedn(extreme temperature-heat) -chaperone proteins are unable to adapt and reshape proteins in time.
Thus, proteins play an important role in the cells of living organisms in various aspects of its molecular composition.
Thank you,
David van der Merwe (u14003262)

By David van der … (not verified) on 23 Apr 2014 #permalink

This just goes to show how complicated life is and how devoted we are in our search for answers.
This particular finding illustrates that evolution can be influenced by even the smallest or even strangest thing. Who would've thought that a heat shock protein can influence eyesight and eye size?
This is an example of how difficult the studying of evolutionary capacitors can be, as they come in many different forms and are utterly unpredictable in how they show themselves.

By u14008395 (not verified) on 28 Apr 2014 #permalink

This post is just incredible. It is amazing to see that a protein can help an organism adapt so quickly to its environment. This HSP90 is extraordinary.

To think that one protein can affect the entire organism by changing it completely so that it can survive. Evolution is remarkable.

Reading this made me think of other organisms and how the HSP90 will affect them when they are placed in new environments wit the need to survive?. How will the evolve?

This is an interesting field of study. I really enjoyed reading this post. I learned something new and very interesting.

By A. Kloppers 14006368 (not verified) on 01 May 2014 #permalink

This post is just incredible. It is amazing to see that a protein can help an organism adapt so quickly to its environment. This HSP90 is extraordinary.

To think that one protein can affect the entire organism by changing it completely so that it can survive. Evolution is remarkable.

Reading this made me think of other organisms and how the HSP90 will affect them when they are placed in new environments with the need to survive?. How will they evolve?

This is an interesting field of study. I really enjoyed reading this post. I learned something new and very interesting.

By A. Kloppers 14006368 (not verified) on 01 May 2014 #permalink

This protein has the ability to stimulate change in the phenotype of an organism which lead them to survive in their habitat. in this case the fishes lost their eye sight but this loss worked at their advantage ,as Dr Dolittle stated that the fishes were able adapt to life in caves.

The changes in phenotype of the fishes which was caused by Hsp90 to this generation will be passed on to their offsprings and enhance the ability of the next generation to withstand the some of the threats in the caves. therefore in conclusion the Hsp90 caused the fishes to evolve.

By u14211816 (not verified) on 02 May 2014 #permalink

Take an organisms ability to survive in a unknown environment, namely how they are less efficient . This obviously would cause stress as the life form would be "pushed into a corner" and forced to adapt, beyond the point of what natural selection allowed it to. I see how this could be possible but would the adaption be passed on to their offspring? (would the organisms genotype be effected?)

By Calvin Wright … (not verified) on 04 May 2014 #permalink