Specificity of Signal-Binding via Non-AHL LuxR-Type Receptors

Autoren

Sophie Brameyer
Ralf Heermann

DOI

10.1371/journal.pone.0124093

Editoren

Jens Kreth

eISSN

1932-6203

Ausgabe der Veröffentlichung

4

Zeitschrift

PLOS ONE

Sprache

en

Online publication date

2015

Paginierung

e0124093 - e0124093

Status

Published online

Herausgeber

Public Library of Science (PLoS)

Herausgeber URL

http://dx.doi.org/10.1371/journal.pone.0124093

Datum der Datenerfassung

2022

Titel

Specificity of Signal-Binding via Non-AHL LuxR-Type Receptors

Ausgabe der Zeitschrift

10

Datenquelle: Crossref

Abstract

Quorum sensing is a typical communication system among Gram-negative bacteria used to control group-coordinated behavior via small diffusible molecules dependent on cell number. The key components of a quorum sensing system are a LuxI-type synthase, producing acyl-homoserine lactones (AHLs) as signaling molecules, and a LuxR-type receptor that detects AHLs to control expression of specific target genes. Six conserved amino acids are present in the signal-binding domain of AHL-sensing LuxR-type proteins, which are important for ligand-binding and -specificity as well as shaping the ligand-binding pocket. However, many proteobacteria possess LuxR-type regulators without a cognate LuxI synthase, referred to as LuxR solos. The two LuxR solos PluR and PauR from Photorhabdus luminescens and Photorhabdus asymbiotica, respectively, do not sense AHLs. Instead PluR and PauR sense alpha-pyrones and dialkylresorcinols, respectively, and are part of cell-cell communication systems contributing to the overall virulence of these Photorhabdus species. However, PluR and PauR both harbor substitutions in the conserved amino acid motif compared to that in AHL sensors, which appeared to be important for binding the corresponding signaling molecules. Here we analyze the role of the conserved amino acids in the signal-binding domain of these two non-AHL LuxR-type receptors for their role in signal perception. Our studies reveal that the conserved amino acid motif alone is essential but not solely responsible for ligand-binding.

Addresses

Biozentrum, Bereich Mikrobiologie, Ludwig-Maximilians-Universität München, Martinsried/München, Germany.

Autoren

Sophie Brameyer
Ralf Heermann

DOI

10.1371/journal.pone.0124093

eISSN

1932-6203

Externe Identifier

PubMed Identifier: 25923884
PubMed Central ID: PMC4414361

Open access

true

ISSN

1932-6203

Ausgabe der Veröffentlichung

4

Zeitschrift

PloS one

Schlüsselwörter

Photorhabdus
Bacterial Proteins
Trans-Activators
Transcription Factors
Repressor Proteins
Ligands
Gene Expression Regulation, Bacterial
Amino Acid Motifs
Conserved Sequence
Quorum Sensing
Acyl-Butyrolactones

Sprache

eng

Medium

Electronic-eCollection

Online publication date

2015

Open access status

Open Access

Paginierung

e0124093

Datum der Veröffentlichung

2015

Status

Published

Publisher licence

CC BY

Datum der Datenerfassung

2015

Titel

Specificity of Signal-Binding via Non-AHL LuxR-Type Receptors.

Sub types

Research Support, Non-U.S. Gov't
research-article
Journal Article

Ausgabe der Zeitschrift

10

Files

https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0124093&type=printable https://europepmc.org/articles/PMC4414361?pdf=render

Datenquelle: Europe PubMed Central

Abstract

Quorum sensing is a typical communication system among Gram-negative bacteria used to control group-coordinated behavior via small diffusible molecules dependent on cell number. The key components of a quorum sensing system are a LuxI-type synthase, producing acyl-homoserine lactones (AHLs) as signaling molecules, and a LuxR-type receptor that detects AHLs to control expression of specific target genes. Six conserved amino acids are present in the signal-binding domain of AHL-sensing LuxR-type proteins, which are important for ligand-binding and -specificity as well as shaping the ligand-binding pocket. However, many proteobacteria possess LuxR-type regulators without a cognate LuxI synthase, referred to as LuxR solos. The two LuxR solos PluR and PauR from Photorhabdus luminescens and Photorhabdus asymbiotica, respectively, do not sense AHLs. Instead PluR and PauR sense alpha-pyrones and dialkylresorcinols, respectively, and are part of cell-cell communication systems contributing to the overall virulence of these Photorhabdus species. However, PluR and PauR both harbor substitutions in the conserved amino acid motif compared to that in AHL sensors, which appeared to be important for binding the corresponding signaling molecules. Here we analyze the role of the conserved amino acids in the signal-binding domain of these two non-AHL LuxR-type receptors for their role in signal perception. Our studies reveal that the conserved amino acid motif alone is essential but not solely responsible for ligand-binding.

Date of acceptance

2015

Autoren

Sophie Brameyer
Ralf Heermann

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/25923884

DOI

10.1371/journal.pone.0124093

eISSN

1932-6203

Externe Identifier

PubMed Central ID: PMC4414361

Ausgabe der Veröffentlichung

4

Zeitschrift

PLoS One

Schlüsselwörter

Acyl-Butyrolactones
Amino Acid Motifs
Bacterial Proteins
Conserved Sequence
Gene Expression Regulation, Bacterial
Ligands
Photorhabdus
Quorum Sensing
Repressor Proteins
Trans-Activators
Transcription Factors

Sprache

eng

Country

United States

Paginierung

e0124093

PII

PONE-D-15-02217

Datum der Veröffentlichung

2015

Status

Published online

Datum, an dem der Datensatz öffentlich gemacht wurde

2016

Titel

Specificity of Signal-Binding via Non-AHL LuxR-Type Receptors.

Sub types

Journal Article
Research Support, Non-U.S. Gov't

Ausgabe der Zeitschrift

10

Datenquelle: PubMed

Specificity of Signal-Binding via Non-AHL LuxR-Type Receptors

Files

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