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PLoS One. 2014 Apr 11;9(4):e89502. doi: 10.1371/journal.pone.0089502. eCollection 2014.

Interaction of a partially disordered antisigma factor with its partner, the signaling domain of the TonB-dependent transporter HasR.

Author information

1
Institut Pasteur, Unité de RMN des Biomolécules, Département de Biologie Structurale et Chimie, Paris, France; CNRS, UMR 3528, Paris, France; Université Pierre et Marie Curie, Cellule Pasteur UPMC, Paris, France.
2
Institut Pasteur, Unité de RMN des Biomolécules, Département de Biologie Structurale et Chimie, Paris, France; CNRS, UMR 3528, Paris, France.
3
Institut Pasteur, Plate-forme de Biophysique des Macromolécules et de leurs Interactions, Département de Biologie Structurale et Chimie, Paris, France.
4
Institut de Biologie Physico-Chimique, CNRS Université Paris-Diderot UMR 7099, Paris, France.

Abstract

Bacteria use diverse signaling pathways to control gene expression in response to external stimuli. In Gram-negative bacteria, the binding of a nutrient is sensed by an outer membrane transporter. This signal is then transmitted to an antisigma factor and subsequently to the cytoplasm where an ECF sigma factor induces expression of genes related to the acquisition of this nutrient. The molecular interactions involved in this transmembrane signaling are poorly understood and structural data on this family of antisigma factor are rare. Here, we present the first structural study of the periplasmic domain of an antisigma factor and its interaction with the transporter. The study concerns the signaling in the heme acquisition system (Has) of Serratia marcescens. Our data support unprecedented partially disordered periplasmic domain of an anti-sigma factor HasS in contact with a membrane-mimicking environment. We solved the 3D structure of the signaling domain of HasR transporter and identified the residues at the HasS-HasR interface. Their conservation in several bacteria suggests wider significance of the proposed model for the understanding of bacterial transmembrane signaling.

PMID:
24727671
PMCID:
PMC3984077
DOI:
10.1371/journal.pone.0089502
[Indexed for MEDLINE]
Free PMC Article
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