Protein Regulation, By Design | October 20, 2008 Issue - Vol. 86 Issue 42 | Chemical & Engineering News
Volume 86 Issue 42 | p. 51 | Concentrates
Issue Date: October 20, 2008

Protein Regulation, By Design

Department: Science & Technology
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Network of linked amino acids (blue) connects dihydrofolate reductase's active site to its surface, providing hot spots for coupling its activity to that of another protein.
Credit: Benkovic Lab/Penn State
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Network of linked amino acids (blue) connects dihydrofolate reductase's active site to its surface, providing hot spots for coupling its activity to that of another protein.
Credit: Benkovic Lab/Penn State

By connecting two proteins at "hot spots" on their surfaces, researchers have designed a hybrid protein in which the activity of one protein is controlled by that of the other (Science 2008, 322, 438). This type of construct may prove to be a general strategy to engineer regulation into proteins, which could be useful for controlling enzymes in industrial bioreactor settings. Rama Ranganathan of the University of Texas Southwestern Medical Center, Stephen J. Benkovic of Pennsylvania State University, and coworkers borrowed a light-sensing protein module from the oat plant to influence the activity of a dihydrofolate reductase enzyme from Escherichia coli. They used statistical coupling analysis, a computational method pioneered by Ranganathan, to find physically connected networks of amino acid residues that link each protein's active site to surface-exposed residues. They next made several hybrid proteins, each linked at different locations. Shining white light on the hybrids doubled the enzyme's activity, but only when the proteins were connected via specific surface hot spots. The team now plans to determine how the signal travels from the light-sensing module to the enzyme.

 
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