UB team describes new biochemistry for RNA at low temperatures







Ribonucleic acid (RNA) is a biological molecule with crucial functions in the genetics of organisms and plays a key role in the origin and evolution of life. With a composition quite similar to DNA, RNA is able to perform a variety of biological functions conditioned by its spatial conformation, i.e. the way the molecule folds in on itself. Now, a paper published in the journal Proceedings of the National Academy of Sciences (PNAS) describes for the first time how the process of RNA folding at low temperatures may open up a novel perspective on primordial biochemistry and the evolution of life on the planet.

The study is led by Professor Fèlix Ritort, from the Faculty of Physics and the Institute of Nanoscience and Nanotechnology (IN2UB) of the University of Barcelona, and is also signed by UB experts Paolo Rissone, Aurélien Severino and Isabel Pastor.

New biochemistry for RNA at low temperatures

RNA is formed by linking molecules of ribose (a monosaccharide) with phosphate groups that bind to four types of nitrogenous bases: adenine (A), guanine (G), cytosine (C) and uracil (U). Both the sequence of bases and the three-dimensional structure of RNA are determining factors in the great versatility of functions that characterize the molecule.

The team used the mechanical unfolding of RNA to understand precisely the diverse forms that RNA takes when it folds in on itself.

The study reveals that RNA sequences that create hairpin structures begin to adopt new, compact structures below 20°C.

“All the RNA molecules studied share unexpected novel structures at low temperatures”, Ritort notes. “We identified a range of temperatures between +20°C and -50°C. Below +20°C, ribose-water interactions start to become important, and a maximum of RNA stability is reached at +5°C, where the density of water is maximal. Below 5ºC, the new RNA stability is determined by ribose-water interactions until -50ºC, when the RNA unfolds again, leading to the phenomenon of cold denaturation”.

The paper hypothesizes that this temperature range is universal and common to all RNA molecules, although it is modulated by sequence and other environmental conditions such as salt and acidity of the medium.

These RNA ranks are simple structures stabilized by the formation of complementary base pairs, in which adenine binds to uracil (A-U) and guanine binds to cytosine (G-C). The researchers believe that these new structures “are created due to the formation of hydrogen bonds between ribose and water that weigh as much or more than the interactions between complementary bases in RNA (A-U and G-C)”. “In fact, — adds Ritort —, “this phenomenon is only observed in RNA, whereas it is not observed in DNA, where the proton at the 2’ position of deoxyribose does not form hydrogen bonds with water”.

To reach their conclusions, the team applied the technique of optical tweezer force spectroscopy, a fine and precise technique for measuring molecular thermodynamics. This technique has made it possible to measure entropy changes and heat capacity during the folding of different RNAs. Therefore, it detects a decrease in the heat capacity of the folded state around 20°C, indicating a reduction in the number of degrees of freedom of the folded RNA (probably due to the effect induced by the ribose-water bonds).

Beyond the traditional view of RNA

But what implications might this phenomenon have for the biochemistry and biological functions of RNA? A first point to note is that the dominance of ribose-water interactions represents an alteration of the hitherto known rules that determine how RNA biochemistry is stabilized by A-U and G-C pairing and base-to-base stacking forces.

The UB professor adds that “this new altered biochemistry that we define in the article has implications for organisms that inhabit cold regions of the Earth (psychrophiles), from alpine regions to the deep waters of the oceans and arctic territories, at temperatures below 10ºC in the eutectic phase of saline water”.

Beyond the specific A-U and G-C pairing rules, “the new RNA biochemistry determined by ribose-water interactions indicates the existence of a primitive, coarse biochemistry based on ribose and other sugars that predates that of RNA itself, which we have called the sweet-RNA world. This primitive biochemistry possibly began to evolve in cold environments in vast outer space, most likely on celestial bodies close to stars and subject to thermal cycles of heat and cold”, concludes Ritort.


Website: Global Innovation Technologist Awards

#Biochemistry #Sciencefather #Research award #MolecularBiology, #Proteomics, #Metabolomics, #EnzymeKinetics, #CellBiology, #BiochemicalResearch, #ProteinStructure, #Genomics, #BiochemicalEngineering, #StructuralBiology, #SystemsBiology, #BiochemicalPathways, #ChemicalBiology, #Bioinformatics, #Pharmacology, #DrugDesign, #BiochemicalAnalysis, #MetabolicPathways #Professor, #Lecturer, #Scientist, #Scholar, #Researcher, #Analyst, #Engineer, #Technician, #Coordinator, #Specialist, #Writer, #Assistant, #Associate, #Biologist, #Chemist, #Physicist, #Statistician, #DataScientist

Visit Our Website : innovationtechnologist.com

Get Connected Here:
==================
Social Media Link

Comments

Post a Comment

Popular posts from this blog

Biochemists create protocells to explore how lipids may have led to first cell membranes

Image
A team of biochemists at the University of California, San Diego, working with a group of biochemical engineers from the University of California, Los Angeles, has found that the development of short lipids might have led to the development of the first cell membranes on early Earth. In their study published in the journal Nature Chemistry , the group combined cysteine with chemical relatives of fatty acids to form lipids with two tails, finding clues about the origins of life on Earth. The research team reasoned that for cells to get their start on early Earth, some form of cell boundary must have formed first to protect cell contents from the environment. Noting that modern cell membranes are all made of lipids, the researchers wondered if the first cell membranes might have been made of lipids as well—and if that was the case, how they might have developed from simple molecules. They also noted that modern cell membranes are complex and generally long chained. Suspecting that earl...
Read more

From chaos to order: Proteins can re-structure themselves to create important substances

Image
The protein 'MIPS' changes its internal structure when it becomes active. Its disordered active centre becomes a defined structure with special functions. The protein plays a key role in the production of inositol, which is also known as vitamin B8, and fulfils important tasks in the body. Researchers at Martin Luther University Halle-Wittenberg (MLU) and the National Hellenic Research Centre in Greece have succeeded for the first time in observing the protein as it re-structures. As the team reports in the scientific journal 'Proceedings of the National Academy of Sciences' (PNAS) this process appears to occur in many similar proteins. Proteins control all vital processes in every organism, for example growth and metabolism. A basic principle of protein research is that the structure of each protein determines its function. If the structure is impaired at just one specific point, the protein can no longer fulfil its function. In the human body, this can lead, for exam...
Read more

Amie Boal named Nicholas and Gelsa Pelick Family Chair in Science

Image
UNIVERSITY PARK, Pa. — Amie Boal, professor of chemistry and of biochemistry and molecular biology, has been named the Nicholas and Gelsa Pelick Family Chair in Science . The purpose of the endowed faculty chair is to provide an outstanding biochemist in the Department of Chemistry or the Department of Biochemistry and Molecular Biology with the resources needed to continue and further their contributions to research , teaching and public service. “I am extremely pleased that we can recognize Amie’s accomplishments and many contributions to Penn State with this well-deserved appointment,” said Mary Beth Williams, acting dean of the Eberly College of Science, James and Alvina Balog Faculty Fellow in Science , and professor of chemistry . “Amie was chosen for her exceptional research , teaching and service to the Department of Chemistry and the Eberly College of Science. She is an integral part of the college’s commitment to excellence and I’m certain that will continue with this new ap...
Read more