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Biochemists identify protease substrates important for bacterial growth and development

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Posted June 28, 2013
Caulobacter crescentus (above) generates radically different cell types upon division. The ClpXP protease (illustrated below) recognizes and destroys many protein substrates that allow Caulobacter to differentiate into these different cell types. New work identifying scores of new candidate substrates of ClpXP to reveal how protein degradation is critical to cell cycle progression and bacterial development could lead to new antibiotic targets. Credit: Peter Chien, UMass Amherst

Caulobacter crescentus (above) generates radically different cell types upon division. The ClpXP protease (illustrated below) recognizes and destroys many protein substrates that allow Caulobacter to differentiate into these different cell types. New work identifying scores of new candidate substrates of ClpXP to reveal how protein degradation is critical to cell cycle progression and bacterial development could lead to new antibiotic targets. Credit: Peter Chien, UMass Amherst

Reporting this month in Molecular Microbiology, Peter Chien and colleagues at the University of Massachusetts Amherst describe using a combination of biochemistry and mass spectrometry to “trap” scores of new candidate substrates of the protease ClpXP to reveal how protein degradation is critical to cell cycle progression and bacterial development. The new understanding could lead to identifying new antibiotic targets.

As Chien (pronounced Chen) explains, to carry out fundamental life processes such as growing and dividing, cells must orchestrate, in time and location, the production and degradation of hundreds of protein substrates. Even in simple bacteria, protein degradation is critical for making sure these organisms can grow and respond to their environment properly.

Scientists have known that a group of protein machines called energy-dependent proteases are responsible for the majority of this degradation, but what targets these machines recognize and how they do it has been unknown in many cases.

With the new series of experiments in the model bacteria Caulobacter crescentus in the Chien biochemistry and molecular biology laboratory, much more is now understood, he says. “We first generated a protease mutant that could recognize but not destroy its targets, acting as a ‘trap’ for protease substrates. After purifying this trap from living cells, we used mass spectrometry to identify proteins that were caught, finding over a hundred new candidate substrates. These targets covered all aspects of bacterial growth, including DNA replication, transcription and cytoskeletal changes.”

Read more at: Phys.org

 

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