New study gives a better understanding of how housekeeping takes place
in cells

Date:
December 9, 2021
Source:
University of Gothenburg
Summary:
Normal household waste is collected and disposed of by waste
collectors, and a similar process occurs in cells to remove damaged
and potentially harmful proteins. A new research study provides
a better understanding of how this is done.



FULL STORY ========================================================================== Normal household waste is collected and disposed of by waste collectors,
and a similar process occurs in cells to remove damaged and potentially
harmful proteins. A new research study in Science Advances provides a
better understanding of how this is done.


==========================================================================
The cells use proteases for housekeeping in almost the same way as waste collectors dispose of household waste.

"Think about what happens when waste collectors go on strike in a
big city.

Similarly, a non-functioning waste collection system in a cell can lead to chaos when damaged proteins accumulate. This could allow serious diseases
to develop," says Bjo"rn M. Burmann, senior lecturer and researcher
in chemistry at the University of Gothenburg, and team leader for the researchers behind the new study.

Neutralises harmful proteins The researchers used the single-cell
bacterium Escherichia coli as a model system to gain a better
understanding of how proteases keep cells clean. This is a bacterium
that is found in the human intestine that has adapted to survive under
a range of stressful environmental conditions.

"One of the waste collection disposal workers in the bacterial cell is the enzyme DegP, a protease that can eliminate unstable and harmful proteins
by shredding them into pieces and thus prevent them from building up
in the cell," says Darius Sulskis, principal author of the study and
doctoral student in Bjo"rn M. Burmann's research group.

Temperature switches activate response Until now it was unknown what
activated DegP, but Darius Sulskis has shown in the study that DegP is activated by a temperature switch is controlled at a molecular level. DegP
is inactive at low temperatures but activates at high temperatures. This
starts up the waste disposal work in the cell, disposing of hazardous
rubbish.

"Understanding this built-in cleaning mechanism means that it can be used
in medical research and be important for future medical applications,"
says Bjo"rn M. Burmann.

Facts Proteases are enzymes, biological catalysts, that facilitate
proteolysis, decomposition of proteins into smaller parts, such as
peptides or even individual amino acids. The research was conducted
using Nuclear magnetic Resonance in the advanced NMR spectroscopy infrastructure at the Swedish NMR Centre, which is hosted by the
University of Gothenburg. The study is the work of researchers from
the University of Gothenburg and the Wallenberg Centre of Molecular and Translational Medicine. The research was made possible by funding from the
Knut and Alice Wallenberg Foundation (BMB), the Swedish Research Council
(BMB) and an EMBO Long-term Fellowship to co-author Johannes Thomas.

========================================================================== Story Source: Materials provided by University_of_Gothenburg. Note:
Content may be edited for style and length.


========================================================================== Journal Reference:
1. Darius Sulskis, Johannes Thoma, Bjo"rn M. Burmann. Structural
basis of
DegP protease temperature-dependent activation. Science Advances,
2021; 7 (50) DOI: 10.1126/sciadv.abj1816 ==========================================================================

Link to news story: https://www.sciencedaily.com/releases/2021/12/211209095639.htm

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