Biochemist professor observes ribosomal rotation more precise with smFRET

Sheikh Jallow

Peter Cornish, associate professor of biochemistry from the University of Missouri, uses a baseball analogy to explain the underlining purpose of his research.

“A baseball can go through different speed and different trajectory,” he said. “The only difference is how you hold the ball. There are many structural transitions that occur within the ribosome that contribute to what state it’s on. It’s always the same ribosome except for minor changes in conformation.”

Funded by the National Science Foundation, Pew Research Center and Wallace Coulter Foundation, Cornish and his graduate students worked in the Cornish Lab, where the main focus of the research was to determine the influence that the complex conformational motions of the ribosome relates to its function using single molecule forster resonance energy transfer, coined as smFRET.

A single molecule forster resonance energy transfer is a technique used to measure the distances between biomolecules. The Cornish Lab studied the motion of the ribosome by injecting it with two dye molecules, hence observing the distances between them with respect to their rotation.

Ribosomes are spherically structured cytoplasmic molecules composed of messenger RNA and protein, which acts as a site for protein synthesis. For example, proteins that our body needs, like bone marrow, are created with the aid of ribosomes.

Scientists have been trying to understand the rotational pattern of ribosomes because the ability to predict the motions of the ribosome exposed to different variables has the potential for numerous breakthroughs.

With the help of past data and various contributors, Cornish’s research team was able to detect a 10-degree constant rotational motion by the ribosome.

However, the study unraveled some unusual pattern of rotation that would require further analysis. Nevertheless, observing the rotation of the ribosome and relating it back to its function renders an optimistic future in creating the possibility to further manipulate the function of the protein synthesis.    

Antibiotics are examples of protein manipulation whereby it combines with the ribosome to stop protein synthesis of bacteria. For Cornish, this precise observation technique could possibly help us understand the synthesis of diseases.

“If one day we figure out how to specifically inhibit protein synthesis in cancer cells, we will cure cancer,” Cornish said. 

Cutlines: Scientists can finally observe the precise rotational motion of ribosomes using smFRET.