Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA (Q27641084)

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3 November 2019

title

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

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3 November 2019

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6

Carol A Gross

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3 November 2019

author name string

Jonathan L Tupy

2

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3 November 2019

Tanja M Gruber

3

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3 November 2019

Sheng Wang

4

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3 November 2019

Meghan M Sharp

5

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Seth A Darst

7

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publication date

1 April 2003

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3 November 2019

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3 November 2019

volume

11

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issue

4

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3 November 2019

page(s)

1067-1078

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Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement

3 November 2019

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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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RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE interaction in the cytoplasm and the availability of sigmaE.RNA polymerase.

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The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28

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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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Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals

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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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Consolidated OpenCitations Corpus – April 2017

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3 November 2019

4504423

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

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