University of Gothenburg<\/a>, outlines the cellular clean-up process from a molecular level.<\/h2>\nIn the real world, waste is normally disposed of and a similar process also needs to be achieved within the biological context of the cell to get rid of broken and possible harmful proteins. Where this task would be achieved in the outside world by a cleaning team, this job is carried out in cells by proteins known as proteases. These proteases work in close relationship to another class of proteins, molecular chaperones, that might be able to rescue and salvage some misfolded proteins to regain their functionality. These processes are of great importance for the cellular fitness, as you can imagine what happens when a maintenance crew is on strike in a big city. A non-functional system in the cells can also directly lead to a non-functional cell through the accumulation of broken proteins, a problem found at the onset of a wide range of severe diseases.<\/p>\n
Maintaining cellular fitness<\/h3>\n
Researchers from the Department of Chemistry and Molecular Biology and the Wallenberg Centre for Molecular and Translational Medicine of the University of Gothenburg, Sweden, used Escherichia coli<\/em>\u00a0 \u2013 a bacterium found in the human gut microbiota that has adapted to survive under a wide variety of different environmental stress conditions \u2013 as a model system. Within this bacterial species, one of the main components of the bacterial stress response to heat is an enzyme called DegP \u2013 a protease which can shred unstable proteins to prevent them from accumulating in the cell envelope of bacteria. DegP is inactive at low temperatures and only becomes active at elevated temperatures, however, the molecular mechanism underlying its activation remained unknown so far.<\/p>\n