DegP primarily functions as a protease for the biogenesis of β‐barrel outer membrane proteins in the Gram‐negative bacterium Escherichia coli. (15th January 2014)

Record Type:: Journal Article
Title:: DegP primarily functions as a protease for the biogenesis of β‐barrel outer membrane proteins in the Gram‐negative bacterium Escherichia coli. (15th January 2014)
Main Title:: DegP primarily functions as a protease for the biogenesis of β‐barrel outer membrane proteins in the Gram‐negative bacterium Escherichia coli
Authors:: Ge, Xi
Wang, Rui
Ma, Jing
Liu, Yang
Ezemaduka, Anastasia N.
Chen, Peng R.
Fu, Xinmiao
Chang, Zengyi
Abstract:: <abstract abstract-type="main" id="febs12701-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="febs12701-sec-0001" sec-type="section"> <p>DegP (also designated as HtrA) and its homologs are found in prokaryotic cells and such eukaryotic organelles as mitochondria and chloroplasts. DegP has been found to be essential for the growth of Gram‐negative bacteria under heat shock conditions and arguably considered to possess both protease and chaperone activities. The function of DegP has not been clearly defined. Using genetically incorporated non‐natural amino acids as photo‐crosslinkers, here we identified the β‐barrel outer membrane proteins (OMPs) as the major natural substrates of DegP in <italic>Escherichia coli</italic> cells. We also demonstrated that DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded OMPs, with hardly any appreciable chaperone activity in cells. We also found that the toxic and cell membrane‐damaging misfolded OMPs would accumulate in DegP‐lacking cells cultured under heat shock conditions. Together, our study defines the primary function of DegP in OMP biogenesis and offers a mechanistic insight into the essentiality of DegP for cell growth under heat shock conditions.</p> </sec> <sec id="febs12701-sec-0002" sec-type="section"> <title>Structured digital abstract</title> <p> <list id="febs12701-list-0001" list-type="bullet"> <list-item> <p> <ext-link ext-link-type="uri" … (more)
Is Part Of:: FEBS journal. Volume 281:Number 4(2014)
Journal:: FEBS journal
Issue:: Volume 281:Number 4(2014)
Issue Display:: Volume 281, Issue 4 (2014)
Year:: 2014
Volume:: 281
Issue:: 4
Issue Sort Value:: 2014-0281-0004-0000
Page Start:: 1226
Page End:: 1240
Publication Date:: 2014-01-15
Subjects:: Biochemistry -- Periodicals
Molecular biology -- Periodicals
Pathology, Molecular -- Periodicals
572
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DOI:: 10.1111/febs.12701 ↗
Languages:: English
ISSNs:: 1742-464X
Deposit Type:: Legaldeposit
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