Genetic Modifications Cause Beetle Wings to Appear on their Abdomen

The New York Times highlights an article published in the Proceedings of the National Academy of Science on how beetles can have genetically modified wings. Dr. Tomoyasu, an evolutionary biologist at the University of Miami, and David Linz have altered the common beetle to have more than two sets of wings on their back. These wings have been genetically engineered to be housed on their abdomen while the beetle is in the larva stage. Since there is a lack of fossil evidence, its hard to tell exactly when insects first took flight (estimated to be approximately 300 million years ago). Some scientists think that insect wings were formed by the fusion of two tissues. The “dual origin” hypothesis of 1974 states that the wings of insects formed when the dorsal body wall and the leg segments fused together. There is some evidence to prove this since some insects have lost the capability of their legs since they have ascended into the body, and some have had them located to their head, which created the antennas. Master switches in the beetle’s genome were manipulated which let the scientists alter which area of the body would have wing growth, however this also altered anatomical structures to the beetle that did not relate to flight at all. GFP (green fluorescent protein) was also introduced to the beetle to mark where the expressions of certain genes were relating to flight.

This article was a good read. Since working with GFP in the lab it is interesting to see the protein being used on a much larger scale level and how it can be used for genetic manipulation in the laboratory setting.

(Related Article)

How Ribosomes Shape the Proteome

Cells are crowded with macromolecules, which restricts the diffusion of proteins, especially in prokaryotic cells without active transport in the cytoplasm. While examining the relationship between crowding, ionic strength and protein diffusion, University of Groningen biochemists made a fascinating discovery: positively charged proteins stick to the surface of ribosome complexes. This explains why most water-soluble proteins carry an overall negative charge. The speed of movement of proteins inside cells is important; many procedures in biological cells depend on interactions between macromolecules (proteins and nucleic acids) and so on their ability to find each other. One of the professor from the University of Groningen stated that the cell cytoplasm is an active place and this will affect protein and RNA diffusion. His team observed the effects of flocking on diffusion, and found a correlation between protein size and diffusion speed. The team then used three different prokaryotes with increasing ionic strength: “the Gram-negative bacterium Escherichia coli, the Gram-positive Lacto coccus lactis and the extremophile Haloferax volcanii, which lives at very high salt concentrations” (University of Groningen). 

Different variants of Green Fluorescent Protein (GFP) with surface charges were constructed, and then the movement of these GFP variants in the three different cell types. They observed that positively charged proteins would diffuse very slowly then, as the further studies were going on it showed that the positive proteins did not bind to the DNA or the cell membrane but to the ribosome complex. The new and unexpected insight that protein movement is a function of protein charge may explain why it is hard to express some proteins in bacterial systems with low ionic strength.  They concluded that a higher ionic strength reduces the stickiness of positively charged proteins and that could be a valuable insight for the construction of protein expression platforms. A final is that the genomes of several endosymbionts show an abundance of positively charged proteins. They said that they have no explanation of how these organisms are able to deal with slow diffusion and ribosomes being engulfed with positive proteins.

References: 

University of Groningen. (2017, December 6). How ribosomes shape the proteome. ScienceDaily. Retrieved December 8, 2017 from www.sciencedaily.com/releases/2017/12/171206100101.htm

How Ribosomes Shape the Proteom. (2017, December 6). Retrieved December 08, 2017, from http://www.sciencenewsline.com/news/2017120614520040.html

What Protein has Changed Biological Studies For the Better?

Everyone has been at the beach and has seen a jellyfish wash up onto the shore or float by you in the ocean. Chances are though, you have never seen a jellyfish glow. A special type of jellyfish called Aequorea Victoria, which is found in the pacific northwest, has a very special trait. This jelly fish can glow! The glow is actually known as  Green Fluorescent Protein (GFP). This protein is solely responsible for the jellyfish's glow. The flow appears around the outer rim of the jellyfish. This protein emits a glow because GFP transduces from energy transfer. The blue chemiluminescence of auqourin into the green fluorescent light. From the discovery of this protein , scientists have been able to use GFP as a tracking agent, which is very interesting. GFP has been inserted into many subjects of study, including other species such as frogs and even humans. Studies done with GFP include attaching it to a protein or cell of study in cancer patients and tracking cells in other diseases.  This protein has significantly advanced biological studies. GFP is an organic substance that is able to work as a tracking devices in cells, and it got rid of dyes, that may have been toxic or altering the function of cells or proteins. For more information you can click on this link.  

Green Fluorescent Protein Biosensors Used to Detect Temperature in Thermal Homeostasis

Homeostasis is the one of the requirements to life. This property is occurring continuously in all living things. Specifically in warm blood animals, thermal homeostasis regulates body temperature. Scientists are interested in the measuring the heat generated from metabolic processes. However, it was not possible to measure the heat generated until researchers created a recombinant fusion protein. This kind of protein was created through genetic engineering a fusion gene, combining TIpA (a protein found in Salmonella) and Green Fluorescent Protein (GFP). TIpA can detect heat changes and attach to the region in the cell while GFP emits green fluorescence. By taking advantage of TIpA's behavior under different temperatures and GFP's ability to fluoresce, the researchers were able to differentiate between hot and cooler temperatures within the cell. According to Principal researcher Yasuo Mori, the next step of the research is to apply it to living model organisms.

Mechanism of TIpA in Hold and Cold Temperatures

Homeostasis is one of the fundamental processes that a living thing undergoes. To understand this process more can help human beings understand the building blocks on life. Sure, this study is only looking for temperature changes, however, I believe that with genetic engineering, other proteins can be developed to track other elements of homeostasis. By further understanding this  process, benefits could be seen to help people who have trouble regulating parts of homeostasis. One must also take into consideration that this is a very early study. But nonetheless, it has the potential to detail the steps taken within homeostasis and help scientists further understand this complex process.