Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease (Q47619672)

4 February 2018

title

Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease (English)

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4 February 2018

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Tim Clausen

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4 February 2018

author name string

Corinna Wilken

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4 February 2018

Karina Kitzing

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4 February 2018

Robert Kurzbauer

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4 February 2018

language of work or name

English

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publication date

1 May 2004

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4 February 2018

published in

Cell

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4 February 2018

volume

117

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4 February 2018

issue

4

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4 February 2018

page(s)

483-494

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4 February 2018

The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor

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DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response

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degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity

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Crystal structure of a PDZ domain

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Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA

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The HtrA Family of Proteases

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The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE.

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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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Proteolysis in prokaryotes: protein quality control and regulatory principles

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Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin

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YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA.

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Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima

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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

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Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi

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Crystal structures of the photosystem II D1 C-terminal processing protease

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The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor

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The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins.

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A novel serine protease of the mammalian HtrA family is up-regulated in mouse uterus coinciding with placentation

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Processing of X-ray diffraction data collected in oscillation mode

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7 January 2021

The HtrA family of serine proteases

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7 January 2021

Structural basis of substrate specificity in the serine proteases

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Periplasmic stress and ECF sigma factors

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2

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DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.

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OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain

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7 January 2021

Posttranslational quality control: folding, refolding, and degrading proteins.

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7 January 2021

Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis

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7 January 2021

A stress sensor for the bacterial periplasm

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7 January 2021

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Identifiers

DOI

1 reference

4 February 2018

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4 February 2018