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Noise in a phosphorelay drives stochastic entry into sporulation in Bacillus subtilis.


ABSTRACT: Entry into sporulation in Bacillus subtilis is governed by a phosphorelay in which phosphoryl groups from a histidine kinase are successively transferred via relay proteins to the response regulator Spo0A. Spo0A~P, in turn, sets in motion events that lead to asymmetric division and activation of the cell-specific transcription factor ?F, a hallmark for entry into sporulation. Here, we have used a microfluidics-based platform to investigate the activation of Spo0A and ?F in individual cells held under constant, sporulation-inducing conditions. The principal conclusions were that: (i) activation of ?F occurs with an approximately constant probability after adaptation to conditions of nutrient limitation; (ii) activation of ?F is tightly correlated with, and preceded by, Spo0A~P reaching a high threshold level; (iii) activation of Spo0A takes place abruptly just prior to asymmetric division; and (iv) the primary source of noise in the activation of Spo0A is the phosphorelay. We propose that cells exhibit a constant probability of attaining a high threshold level of Spo0A~P due to fluctuations in the flux of phosphoryl groups through the phosphorelay.

SUBMITTER: Russell JR 

PROVIDER: S-EPMC5623841 | biostudies-other | 2017 Oct

REPOSITORIES: biostudies-other

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Noise in a phosphorelay drives stochastic entry into sporulation in <i>Bacillus subtilis</i>.

Russell Jonathan R JR   Cabeen Matthew T MT   Wiggins Paul A PA   Paulsson Johan J   Losick Richard R  

The EMBO journal 20170824 19


Entry into sporulation in <i>Bacillus subtilis</i> is governed by a phosphorelay in which phosphoryl groups from a histidine kinase are successively transferred via relay proteins to the response regulator Spo0A. Spo0A~P, in turn, sets in motion events that lead to asymmetric division and activation of the cell-specific transcription factor σ<sup>F</sup>, a hallmark for entry into sporulation. Here, we have used a microfluidics-based platform to investigate the activation of Spo0A and σ<sup>F</s  ...[more]

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