Artefactual cleavage of E coli H-NS by OmpT. (Q54564473)

1 June 2018

title

Artefactual cleavage of E coli H-NS by OmpT. (English)

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1 June 2018

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Goldberg MD

1

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1 June 2018

Canvin JR

2

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Freestone P

3

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Andersen C

4

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Laoudj D

5

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Williams PH

6

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Holland IB

7

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Norris V

8

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publication date

1 June 1997

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1 June 2018

published in

Biochimie

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1 June 2018

volume

79

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issue

6

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1 June 2018

page(s)

315-322

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1 June 2018

Protein H1: a role for chromatin structure in the regulation of bacterial gene expression and virulence?

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The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor.

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Autoregulatory expression of the Escherichia coli hns gene encoding a nucleoid protein: H-NS functions as a repressor of its own transcription.

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H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro

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Escherichia coli DNA-binding protein H-NS is localized in the nucleoid

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Anucleate cell production by Escherichia coli delta hns mutant lacking a histone-like protein, H-NS.

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SecY protein, a membrane-embedded secretion factor of E. coli, is cleaved by the ompT protease in vitro

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In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to a cold environment

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Identifiers

DOI

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1 June 2018

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1 June 2018