Take away the complexities of the life clock

Take away the complexities of the life clock

Figure 1. The circadian rhythms of the phosphorylation circle (red circle with “P” indicating phosphorus transfer) and the ATP hydrolysis circle (blue circle with “ATP” and “ADP” indicate conversion of Adenosine-TriPhosphate to Adenosine-DiPhosphate) to be observed in a test tube. Yes: NINS / IMS

Scientists want to increase their understanding of circadian rhythms, those 24-hour cycles in sleep and wake that are produced in living things, from humans to plants. and in others the bacteria. A team of researchers has looked at the complex activity of cyanobacteria and has now better understand what drives its circadian clock.

The group, led by researchers from the Institute for Molecular Science, National Institutes of Natural Sciences in Okazaki, Japan, published their findings on April 15, 2022 in Scientific advances.

The team focused their research on KaiC, the clock protein that regulates the circadian rhythm in cyanobacteria, a type of bacteria that lives in all aquatic bodies and is often found in blue-green algae. These biological clocks are formed in organisms with proteins. The cyanobacterial circadian clock is the simplest circadian clock according to the number of its parts, but it is a very complex system that can give scientists clues as to the function of all circadian clocks. Red cyanobacteria are microorganisms that can be found in environments from salt and fresh water to soil and rocks. The team looked at the mechanism for allostery, complex changes that underlie the nature and function of the KaiC protein in cyanobacteria. Allostery clears the cyanobacterial circadian clock.

The team studied the atomic structures of the KaiC clock protein, by observing thousands of crystallization stages. This detailed study of atomic structures allows them to cover the entire phosphorylation cycle, which is the process by which a phosphate is transferred to a protein (Figure 2, bottom panel). Phosphorylation is also associated with an endogenous mechanism, ATP hydrolysis, which is the energy dissipation process that determines the clock speed (Figure 2, top panel). The phosphorylation-ATP hydrolysis system acts as a regulator for cell function. To help them understand the origin of the allosstery, they dissolved the KaiC protein in eight different states, allowing them to observe the interaction between the phosphorylation cycle and the hydrolysis cycle. ATP acts in the same way as both (Figure 2, right).

Take away the complexities of the life clock

Figure 2. The phosphorylation environment and the ATP hydrolysis environment in the KaiC secondary ring cell. The two circles are bounded by hydrogen bonds between acids, bases, and inerts. Yes: NINS / IMS

In the past, scientists have studied the phosphorus structure of the KaiC protein in vivio, in vitro, and in silico. However, little is known about the allostery regulation of the phosphorus cycle in KaiC.

By studying the KaiC in eight different states, the team was able to observe a group that stands for the phosphorus cycle and the ATPase hydrolysis cycle. This combination of the two drives the cyanobacterial circadian clock.

“Because proteins are made up of so many atoms, it’s not easy to understand the mechanisms by which they work hard but are ordered. We have to look for changes in proteins with patience, ”said Yoshihiko Furuike, assistant professor at the Institute for Molecular. Science, National Institute of Natural Sciences.

The KaiC protein accelerates and terminates response cycles independently to regulate the association positions of clockwise proteins. So considering their next work, the team could use structural biology to show the atomic characteristics of the speed and deceleration of gear rotations. “Our goal is to detect all clock proteins during oscillation at the atomic level and explain when the command sound comes from the chaotic atomic dynamics,” says Furuike.

Their work could serve as a research tool, helping scientists better understand the processes involved in the circadian clock cycle. Looking ahead, the research team will be able to share their findings with broad applications. Fats, fats, plants, and carbohydrates have their own proteins in a variety of processes and patterns. “However, post -evaluation of the relationship between KaiC dynamics and clock operations can be used in other studies involving different organisms,” says Furuike.


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More information:
Yoshihiko Furuike et al, Elucidation of master allostery necessary for circadian clock oscillation in cyanobacteria, Scientific advances (2022). DOI: 10.1126 / sciadv.abm8990. www.science.org/doi/10.1126/sciadv.abm8990

Presented by National Institutes of Natural Sciences

Directions: Unlocking the complex functions of the biological clock (2022, April 15) Retrieved 15 April 2022 from https://phys.org/news/2022-04-complex-biological-clock.html

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