The study published in Angewandte Chemie sheds light on how ribose may have become the preferred sugar for RNA development, highlighting its unique ability to bind with phosphate more quickly and effectively than other sugar molecules. This characteristic could have played a crucial role in selecting ribose as the building block of life.

Ramanarayanan Krishnamurthy, professor of chemistry at Scripps Research, emphasizes that this finding supports the idea that prebiotic chemistry could have produced the fundamental components of RNA, which eventually led to entities exhibiting lifelike properties. The research focuses on phosphorylation, a step within nucleotide-building where ribose connects to the phosphate group, and explores whether other sugars can undergo similar reactions.

The team’s experiments showed that while diamidophosphate (DAP) could phosphorylate all four sugar molecules tested, it phosphorylated ribose at a significantly faster rate. The reaction with ribose produced exclusively ring-shaped structures with five corners, whereas the other sugars formed a combination of 5- and 6-member rings.

“This really showed us that there is a difference between ribose and the three other sugars,” says Krishnamurthy. “Ribose not only reacts faster than the other sugars, it’s also more selective for the five-member ring form, which happens to be the form that we see in RNA and DNA today.”

When DAP was added to a solution containing equal amounts of the four different sugars, it preferentially phosphorylated ribose. The researchers demonstrated that this selective process produces a molecule with a form conducive for making RNA, providing further evidence for ribose’s preeminence.

While the study does not claim that these reactions directly led to life, it suggests that they might have played a crucial role in the primordial process that gave rise to the fundamental components of life. The researchers caution against over-interpretation and emphasize the need for further investigation into the emergence of life on Earth.

In future research, the team plans to test whether this chemical reaction can occur inside primitive cellular structures called protocells. If successful, it might provide a compelling explanation for how ribose became the preferred sugar for RNA development and ultimately gave rise to life as we know it today.

A groundbreaking study has shed new light on the fundamental mechanisms governing microtubule growth within cells. Researchers from Queen Mary University of London and the University of Dundee have made a significant breakthrough by discovering that the ability of tubulin proteins at microtubule ends to connect with each other sideways determines whether a microtubule elongates or shortens.

Microtubules are crucial protein structures that form the internal skeleton of cells, providing structural support and generating dynamic forces that push and pull. These tiny filaments constantly assemble and disassemble by adding or removing tubulin building blocks at their ends. However, the precise rules dictating whether a microtubule grows or shrinks have long remained a mystery due to the complexity and miniature size of their ends.

The collaborative research team has cracked part of this code using advanced computer simulations coupled with innovative imaging techniques. This interdisciplinary approach has allowed them to address this complex biological question from a fresh perspective, bridging physics and biology.

Dr. Vladimir Volkov, co-lead author from Queen Mary University of London, explained the significance of their findings: “Understanding how microtubules grow and shorten is very important – this mechanism underlies division and motility of all our cells. Our results will inform future biomedical research, particularly in areas related to cell growth and cancer.”

Dr. Maxim Igaev, co-lead author from the University of Dundee, highlighted the power of their interdisciplinary approach: “Bridging physics and biology has allowed us to address this complex biological question from a fresh perspective. This synergy not only enriches both fields but also paves the way for discoveries that neither discipline could achieve in isolation.”

This exciting research deepens our understanding of fundamental cellular processes and opens potential new avenues for biomedical research, particularly in areas concerning cell proliferation and the development of treatments for diseases like cancer.

The inner workings of cells have long been a subject of scientific inquiry, and researchers at Stockholm University’s SciLifeLab have made a groundbreaking discovery. A team led by Professor David Drew has uncovered how the cell’s main energy currency, ATP (adenosine triphosphate), is transported into the endoplasmic reticulum (ER), the cell’s primary “shipping port” for protein and lipid packaging.

The ER plays a vital role in checking protein quality and facilitating their transport within the cell. For these processes to occur efficiently, energy in the form of ATP is required. Despite decades of research on ER function, the question of how ATP reaches the inside of the ER had remained unclear – until now.

Professor Drew’s team confirmed that the transporter protein SLC35B1 is the key gateway for ATP entry into the ER. This discovery was made possible through a combination of biochemical and structural validation, including the use of cryo-electron microscopy (cryo-EM) to visualize SLC35B1 in multiple conformations.

The study published in Nature reveals the first structural and mechanistic insight into how ATP enters the endoplasmic reticulum using the transporter protein SLC35B1. The ER is the cell’s main “shipping port” that packages proteins and lipids, checks their quality, and facilitates their transport within the cell.

“This discovery has broad implications for human health,” says Professor Drew. “Disrupted ER activity is linked to diseases such as type 2 diabetes, cancer, and neurodegenerative disorders, where ER stress and protein misfolding play central roles.” With a detailed molecular blueprint now available, SLC35B1 presents a promising target for future drug development.

Understanding how energy is delivered into the ER gives researchers powerful new ways to tackle these diseases. Modulating SLC35B1 activity could become a new strategy for restoring ER balance in disease states.

Professor Drew’s team has already begun screening for small molecules that modulate SLC35B1 function, with the goal of developing targeted therapies to either enhance or inhibit ATP transport when needed. This research holds great promise for improving human health and unlocking new therapeutic opportunities for diseases linked to ER dysfunction.