Scientists use light to control proteins that catalyze biochemical reactions

October 17th, 2008 - 5:23 pm ICT by ANI  

Washington, October 17 (ANI): A research team comprising of experts from Penn State and the University of Texas Southwestern Medical Center has devised a way to use light to control certain proteins that catalyze biochemical reactions.
“This is one of the first examples of someone successfully controlling the activity of a protein using light,” said Stephen Benkovic, Penn State Evan Pugh Professor of Chemistry, holder of the Eberly Family Chair in Chemistry, and one of the team’’s leaders.
“The technology one day could be expanded to have multiple uses, including the ability to turn off the activities of some disease-causing proteins in the cell,” he added.
For their study, the researchers designed a hybrid protein by inserting a light-sensing protein from an oat plant into an enzyme from the bacterium E.coli.
Once that was done, the researchers observed that the enzymes activity could be manipulated by shining a light on the light-sensing protein.
“The technology works like a light switch. When we shine a light on the light-sensing domain, the enzyme’’s activity increases, and when we shut the light off, the enzyme’’s activity decreases,” said Benkovic.
Jeeyeon Lee, a postdoctoral scholar in the Penn State Department of Chemistry, said that the research group had to consider a number of factors when designing the hybrid protein, including the protein’’s shape, or what is referred to as its conformation.
“The conformation of a protein is important in determining its function. Without the proper conformation, our protein would not have responded to the light,” she said.
The researchers also had to consider the proper location on the enzyme into which the light-sensing protein from the oat plant would be inserted.
They were surprised to see that the switch worked only when they attached the light-sensing domain to the enzyme at a particular site, and not when attached to other locations.
“The fact that the switch worked only when the light-sensing domain was attached to the enzyme at a specific site suggests that a unique network is active at that site through which signals, such as those responding to light, are transmitted,” said Vishal Nashine, also a postdoctoral scholar in the Department of Chemistry and an author of the paper.
The researchers located the successful site among more than a hundred different possibilities by using a computational algorithm called the Statistical Coupling Analysis (SCA).
Their future research will investigate how the signal triggered by the light was transmitted from the light-sensing domain to the enzyme.
“It is not yet clear how this process works. So far, the effect has been small, but we plan to optimize the technology to see if we can use light to modulate the enzyme’’s activity in alternative ways,” said Benkovic.
The results of the study appear in the journal Science. (ANI)

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