amino acid
The amino acid selenocysteine, 3D-balls model. Credit: YassineMrabet/CC BY 3.0/Wikipedia

Scientists have found that a human's ability to detect individual amino acids is the same as that of a bacterium.

It adds to the sparse evidence suggesting there are similarities between humans andbacteria with respect to the presence of essential components of life, such as oxygen and food.

There is no common chemical detection mechanism that is currently known, and the cells have different types of sensors.

Scientists discovered a universal sensor that can be found in many different receptors that can be used to detect the two groups of atoms that are shared by all the amino acids.

For the first time, we have a universal way of detecting amino acids. The senior author of the study said that nearly every organisms can do it through this mechanism.

It is very rare when we can translate a specific sensory function from one life form to another, because these life forms are separated by 3 billion years.

The study was published in the National Academy of Sciences.

Most of the work inside cells is done by the information stored in genes, which are the building blocks of life.

In earlier studies of a bacterium that causes human infections, the lab and partners in Spain found several receptors that recognized the amino acids, and a structural feature that all of the other proteins shared. Vadim Gumerov, a research scientist in the Jouline lab, looked for other organisms that had the same structural feature, called a motif, that he was looking for. Gumerov was able to identify the amino acid-binding motif in human receptors through analysis of sequence and structure information.

The outer-facing segment of the protein that crosses the cell&s outer membrane is where this motif is located. The team combined their computations with experimental data and found that this motif is found in only a few plant species. The analyses showed that all of the motifs bind only the two acids.

The sensor helps the organisms navigate towards a food source.

It is a part of a primitive nervous system forbacteria, which helps them make decisions. We found a sensor in human calcium channels that regulates the release of neurotransmitters. There is a link between calcium channels and pain.

That is where the GABA comes in. Drug developers knew before this study that drugs derived from gyaba could be used to treat pain and other disorders.

It turns out that the research team that found the motif in humans is the same one that found the one that is enabling detection of the amino acids.

The effects of mutating the motif were tested in experiments using a rat that functions the same way as the human one. The function of the entire receptor was changed by changing the motif.

The work shows precisely where the drugs will bind and how they will bind, which is important because now they want to improve it. The two missing points are which part of the drug will bind to which amino acid of theProtein and how it is oriented in 3D space.

Jouline has begun a broader search for sensors that have a role in sustaining life, even though there may never be a definitive answer to the age-old question of what exactlybacteria and humans have in common biologically.

He said that they know where to look, but only at their segments that are involved in recognizing physical and chemical parameters important to all living systems.

More information: Vadim M. Gumerov et al, Amino acid sensor conserved from bacteria to humans, Proceedings of the National Academy of Sciences (2022). DOI: 10.1073/pnas.2110415119 Journal information: Proceedings of the National Academy of Sciences Citation: Scientists make rare discovery of a protein function universal to bacteria and humans (2022, March 1) retrieved 1 March 2022 from https://phys.org/news/2022-03-scientists-rare-discovery-protein-function.html This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no part may be reproduced without the written permission. The content is provided for information purposes only.