Frozen lighting keys: How can microbes in the Arctic a revolution a revolution in neuroscience

Kovalev, EPODODOCTORAL fellow in the Schneider’s Embl Hamburg and Bateman Embl-EBI collection, is passionate about solving biological problems. It is a special drug addict by Rhodopsins, a group of colored proteins that enable aquatic microorganisms to harness the sun’s energy.

“In my work, I am looking for an extraordinary Rhodopsins and try to understand what they are doing,” said Kovalv. “These molecules can have undiscovered functions that we can benefit from.”

Some of Rhodopsins have already been modified to serve as light -acting electrical activity keys in cells. This technique, called optics, is used by neurologists to selectively control nervous activity during experiments. Rhodopsins can be used with other capabilities, such as enzyme activity, to control chemical reactions with light, for example.

After Rhodopsins studied for years, Kovalv believed that he knew them from the inside out – until he discovered a new mysterious group of Rhodopsins, which was unlike anything he had seen before.

As it often happens in science, it started starkly. While browsing the online protein databases, Kovalev monitored a common unusual feature in Rhodopsins microbial microbials exclusively in very cold environments, such as ice flowers and high mountains. “This is strange,” he said. After all, rhodopsins is something you usually find in seas and lakes.

The cold climatic climate Rhodopins was almost identical to each other, although it had evolved thousands of kilometers. This cannot be a coincidence. Kovalv concluded that it is necessary to survive in the cold.

Rhodopsins of blue

Kovalev wanted to find out more: how these Rhodopsins look like, how it works, in particular, what color is.

Color is the main advantage of each rhodopsin. Most of them are orange pink – they reflect pink and orange light, absorb green and blue light, which activates them. Scientists seek to create a different colored Rhodopsins plate, so that they can control more accurate nervous activity. Blue Rhodopsins has been specially searching because it is activated by red light, which penetrates the tissues deeper and not forests.

To the amazement of Kovalev, Cryhodopsins, which he examined in the laboratory revealed an unexpected diversity of colors, and most importantly, some of them were blue.

The color of each rhodopine is determined by its molecular structure, which dictates the wavelengths of the light that absorbs and reflects. Any changes in this structure can change color.

Kovalv laughed: “I can actually know what is going on with Cryorhodopsin simply by looking at its color.”

By applying advanced structural biology techniques, discovered that the secret of blue is the same rare structural feature that it originally monitored in protein databases.

“Now that we understand what makes them blue, we can design the artificial blue -blue Rhodoppines designed for different applications,” said Kovalif.

Next, examine Kovalev Cryorhodopsins in the cultivated brain cells. When cells that express Cryorhodopsins exposed to UV light, they caused electrical currents inside. Interestingly, if the researchers shine the cells then directly with green light, the cells become more exciting, while if they use ultraviolet/red light instead, it has reduced the excitement of the cells.

“The new optical tools to switch the electrical activity of the cell are both efficiently” ON “and” OF “incredibly useful in research, biotechnology and medicine.” “For example, in my group, we develop the new optical cochlear cochlear cultivation for patients who can restore visual hearing in patients. Developing a benefit like this is a multi -purpose Rhodopine for future applications important important for the following studies.”

“Our Cryrhodopsins is not ready to use it as tools yet, but it is an excellent initial model. They have all the main features that can be designed, based on the results we have reached, to become more effective in optical science,” Kovalv said.

Ultraviolet lighting light for development

When exposed to sunlight even on a rainy winter day in Hamburg, Cryorhodopsins can feel ultraviolet radiation, as shown by using the advanced spectral analysis by Kovalev collaborators of Goethe Frankfurt University led by Josef Wachtveitl. The Wachtveitl team showed that Cryhodopsins is actually slower among all Rhodopsins in its ablution. This has made scientists suspect that these Cryorhodopsins may behave like optical materials to allow microbes to “see” ultraviolet light – an unknown property among Cryorhodopsins.

“Can they really do that?” Kovalv remained asking himself. The typical sensor protein cooperates with a messenger molecule that passes the information from the cell membrane inward.

Kovalev has become more convinced, when it is with the collaborators with Alkante, Spain and his partner in Embl-EBI, noticed that the Cryhodopsin gene is always accompanied by a gene that draws a small protein of unknown functions, and may be associated with a functional.

Kovalv asked whether this was the lost Messenger. Using the Ai Alphafold tool, the team enables the team to show that five copies of the small protein will form a loop and interact with Cryorhodsin. According to their predictions, the small protein sits ready against Cryorhodopsin inside the cell. They believe that when Cryorhodopsin discovers UV light, a small protein can leave to carry this information to the cell.

“It has been great to discover a new mechanism through which a sensitive sign of Cryorhodopsins can be transmitted to other parts of the cell. It is always like suspense to know what functions of unusual proteins are. In fact, we also find these proteins in living organisms that do not contain Cryorhodopsin, and may swing in a very wide range of functions.

Why has Cryorhodopsins evolved its amazing dual function – and why only in cold environments – still is a mystery.

“We doubt that Cryrhodopsins has evolved its unique features not because of the cold, but rather allowing microbes to feel ultraviolet rays, which can be harmful to them,” said Kovalif. “In cold environments, such as the top of the mountain, bacteria face a severe radiation of ultraviolet radiation. Cryhodopsins may help them feel it, so that they can protect themselves. This hypothesis is well compatible with the results we have reached.”

“The discovery of unusual molecules like this will not be possible without scientific campaigns to remote sites often, to study the adaptations of living organisms that live there,” Kovalv added. “We can learn a lot!”

A unique approach to unique molecules

To reveal the wonderful biology of Cryorhodopsins, Kovalev and its collaborators have to overcome many technical challenges.

One of them is that Cryorhodopsins is almost identical to the structure, and even a slight change in the position of one atom can lead to different properties. The study of molecules at this level of details requires that the standard experimental methods be overcome. Kovalev applied 4D structural biological approach, combining X-ray crystals in Embl Hamburg Beamline P14 and Cryo (Cryo-AE) in the Albert Juskov group in Greneninin, Netherlands, with protein activation with light.

“I have already chosen to make my mail at Embl Hamburg, because of the preparation of the unique beam line that made my project possible.” “The P14 Beamline team has fully working together to adapt the preparation for my experiences – I am very grateful to help them.”

The other challenge was that Cryrhodopsins is very sensitive to light. For this reason, Kovalev collaborators had to learn to work with samples in almost complete darkness.