Nature
A New Discovery Of Protein Receptor Found In A Family Of Invertebrates
Jeffrey Morcilla
First Posted: Nov 21, 2016 04:14 AM EST
A new photoreceptor has been discovered in a family of invertebrates that is about 50 times more efficient in perceiving light compared in the rhodopsin of the human eye.
According to an international team of scientistis that is led by the University of Michigan, the team discovered a new type of receptor protein called as LITE-1. According to Science Daily, this photoreceptor was discovered in the hollow tube and eyeless roundworm that is classified under the phylum of nematoda -- the nematodes and commonly used for Bioscience research.
Based on the statement released by Shawn Xu -- a professor in the Department of Molecular and Integrative Physiology at the U-M Medical School -- he states that "LITE-1 actually comes from a family of taste receptor proteins first discovered in insects, These, however, are not the same as the taste receptors as in the mammals."
He also suggests that although nematodes lack eyes, still they can be able to move away from the flashes of light. Life Sience also reported that since the photoreceptors convert light into a signal that the body can use, this LITE-1 is "unusual" in that it is extremely efficient absorbing both UV-A and UV-B light -- 10 to 100 times greater than the two other types found in the animal kingdom: opsins and cryptochromes, as mentioned by the professor.
Prof. Xu also added that the genetic makeup of the photoreceptor is also very uncommon from other types of receptor protein, which is usually found in animals, plants and microbes. Therefore, it creates a new gateway of deciphering a puzzle through the intensive research that will use in a variety of ways.
Furthermore, scientists also suggest there might be a possibility of developing LITE-1 into a sunscreen additive that absorbs harmful rays, and for further scientific investigation, it might foster light sensitivity in a new type of cell.
Finally, several characteristics make LITE-1 unusual as compared to the animal photoreceptors that have two components (base protein and light absorbing chromophore). When the protein receptor breaks apart, the chromophore will still work unlike the LITE-1. When this photoreceptor is denatured, it will completely stop its ability to absorb light rather than to diminish it.
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First Posted: Nov 21, 2016 04:14 AM EST
A new photoreceptor has been discovered in a family of invertebrates that is about 50 times more efficient in perceiving light compared in the rhodopsin of the human eye.
According to an international team of scientistis that is led by the University of Michigan, the team discovered a new type of receptor protein called as LITE-1. According to Science Daily, this photoreceptor was discovered in the hollow tube and eyeless roundworm that is classified under the phylum of nematoda -- the nematodes and commonly used for Bioscience research.
Based on the statement released by Shawn Xu -- a professor in the Department of Molecular and Integrative Physiology at the U-M Medical School -- he states that "LITE-1 actually comes from a family of taste receptor proteins first discovered in insects, These, however, are not the same as the taste receptors as in the mammals."
He also suggests that although nematodes lack eyes, still they can be able to move away from the flashes of light. Life Sience also reported that since the photoreceptors convert light into a signal that the body can use, this LITE-1 is "unusual" in that it is extremely efficient absorbing both UV-A and UV-B light -- 10 to 100 times greater than the two other types found in the animal kingdom: opsins and cryptochromes, as mentioned by the professor.
Prof. Xu also added that the genetic makeup of the photoreceptor is also very uncommon from other types of receptor protein, which is usually found in animals, plants and microbes. Therefore, it creates a new gateway of deciphering a puzzle through the intensive research that will use in a variety of ways.
Furthermore, scientists also suggest there might be a possibility of developing LITE-1 into a sunscreen additive that absorbs harmful rays, and for further scientific investigation, it might foster light sensitivity in a new type of cell.
Finally, several characteristics make LITE-1 unusual as compared to the animal photoreceptors that have two components (base protein and light absorbing chromophore). When the protein receptor breaks apart, the chromophore will still work unlike the LITE-1. When this photoreceptor is denatured, it will completely stop its ability to absorb light rather than to diminish it.
See Now: NASA's Juno Spacecraft's Rendezvous With Jupiter's Mammoth Cyclone