Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli. (Q50924387)

25 March 2018

title

Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli. (English)

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4

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Mark J Fogg

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Keith S Wilson

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Tony Wilkinson

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Eiso Ab

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Eiso Ab

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Tammo Diercks

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Tammo Diercks

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author name string

Rosa Grenha

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Neil J Rzechorzek

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James A Brannigan

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Vincent Truffault

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Joanne C Ladds

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Cristina Bongiorni

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Marta Perego

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Robert Kaptein

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Gert E Folkers

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language of work or name

English

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publication date

25 September 2006

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Journal of Biological Chemistry

published in

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volume

281

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issue

49

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page(s)

37993-38003

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Sporulation of Bacillus subtilis

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Isolation and characterization of kinC, a gene that encodes a sensor kinase homologous to the sporulation sensor kinases KinA and KinB in Bacillus subtilis

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Analysis of a suppressor mutation ssb (kinC) of sur0B20 (spo0A) mutation in Bacillus subtilis reveals that kinC encodes a histidine protein kinase

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Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis.

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Deactivation of the sporulation transcription factor Spo0A by the Spo0E protein phosphatase

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A new family of aspartyl phosphate phosphatases targeting the sporulation transcription factor Spo0A of Bacillus subtilis

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Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis

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Evolution of signalling in the sporulation phosphorelay

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21 January 2018

Identifiers

DOI

10.1074/JBC.M607617200

1 reference

25 March 2018

PubMed ID

17001075

1 reference

25 March 2018