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Article ; Online: How an unusual chemosensory system forms arrays on the bacterial nucleoid.

Mauriello, Emilia M F

2020 Volume 48, Issue 2, Page(s) 347–356

Abstract: Chemosensory systems are signaling pathways elegantly organized in hexagonal arrays that confer unique functional features to these systems such as signal amplification. Chemosensory arrays adopt different subcellular localizations from one bacterial ... ...

Abstract	Chemosensory systems are signaling pathways elegantly organized in hexagonal arrays that confer unique functional features to these systems such as signal amplification. Chemosensory arrays adopt different subcellular localizations from one bacterial species to another, yet keeping their supramolecular organization unmodified. In the gliding bacterium Myxococcus xanthus, a cytoplasmic chemosensory system, Frz, forms multiple clusters on the nucleoid through the direct binding of the FrzCD receptor to DNA. A small CheW-like protein, FrzB, might be responsible for the formation of multiple (instead of just one) Frz arrays. In this review, we summarize what is known on Frz array formation on the bacterial chromosome and discuss hypotheses on how FrzB might contribute to the nucleation of multiple clusters. Finally, we will propose some possible biological explanations for this type of localization pattern.
MeSH term(s)	Bacterial Proteins/metabolism ; Chemotaxis ; Chromosomes, Bacterial ; Cytoplasm/metabolism ; Mutation ; Myxococcus xanthus/metabolism ; Phenotype ; Protein Binding ; Signal Transduction
Chemical Substances	Bacterial Proteins ; FrzCD protein, Myxococcus xanthus
Language	English
Publishing date	2020-05-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20180450
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Article ; Online: The differential expression of PilY1 proteins by the HsfBA phosphorelay allows twitching motility in the absence of exopolysaccharides.

Xue, Shuanghong / Mercier, Romain / Guiseppi, Annick / Kosta, Artemis / De Cegli, Rossella / Gagnot, Severine / Mignot, Tâm / Mauriello, Emilia M F

PLoS genetics

2022 Volume 18, Issue 4, Page(s) e1010188

Abstract: ... associated to the M. xanthus cell surface or deposited on the substrate. In this study, a genetic screen ...

Abstract	Type Four Pili (T4P) are extracellular appendages mediating several bacterial functions such as motility, biofilm formation and infection. The ability to adhere to substrates is essential for all these functions. In Myxococcus xanthus, during twitching motility, the binding of polar T4P to exopolysaccharides (EPS), induces pilus retraction and the forward cell movement. EPS are produced, secreted and weakly associated to the M. xanthus cell surface or deposited on the substrate. In this study, a genetic screen allowed us to identify two factors involved in EPS-independent T4P-dependent twitching motility: the PilY1.1 protein and the HsfBA phosphorelay. Transcriptomic analyses show that HsfBA differentially regulates the expression of PilY1 proteins and that the down-regulation of pilY1.1 together with the accumulation of its homologue pilY1.3, allows twitching motility in the absence of EPS. The genetic and bioinformatic dissection of the PilY1.1 domains shows that PilY1.1 might be a bi-functional protein with a role in priming T4P extension mediated by its conserved N-terminal domain and roles in EPS-dependent motility mediated by an N-terminal DUF4114 domain activated upon binding to Ca2+. We speculate that the differential transcriptional regulation of PilY1 homologs by HsfBA in response to unknown signals, might allow accessorizing T4P tips with different modules allowing twitching motility in the presence of alternative substrates and environmental conditions.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Movement/genetics ; Fimbriae Proteins/genetics ; Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/metabolism ; Myxococcus xanthus/physiology
Chemical Substances	Bacterial Proteins ; Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2022-04-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1010188
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Article ; Online: Cell biology of bacterial sensory modules.

Mauriello, Emilia M F

Frontiers in bioscience (Landmark edition)

2013 Volume 18, Issue 3, Page(s) 928–943

Abstract: Despite their small size, bacterial cells possess very efficient sensory apparatus that allow them to perceive and respond to the external environment with cell movement. In enteric bacteria, these apparatus are complex lattices of different ... ...

Abstract	Despite their small size, bacterial cells possess very efficient sensory apparatus that allow them to perceive and respond to the external environment with cell movement. In enteric bacteria, these apparatus are complex lattices of different chemoreceptors working in concert and forming clusters positioned at the cell poles. Since the study of chemotaxis has been expanded to other bacterial species, examples of chemosensory systems regulating functions different than taxis have been described and chemoreceptors localizing in ways divergent from the enteric paradigm have been visualized. The scope of this review is to revise and summarize the architecture of different bacterial chemoreceptors. Then, hypotheses will be proposed on how chemoreceptor distribution in cells is coupled to specific functions and life styles in well-characterized bacterial model systems, such as Escherichia coli, Rhodobacter sphaeroides, Caulobacter crescentus and Myxococcus xanthus.
MeSH term(s)	Bacterial Physiological Phenomena ; Cell Biology ; Cell Cycle
Language	English
Publishing date	2013-06-01
Publishing country	Singapore
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2704569-9
ISSN	2768-6698 ; 1093-9946
ISSN (online)	2768-6698
ISSN	1093-9946
DOI	10.2741/4154
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Article ; Online: Defining Two Chemosensory Arrays in

Fortier, Emma M / Bouillet, Sophie / Infossi, Pascale / Ali Chaouche, Amine / Espinosa, Leon / Giudici-Orticoni, Marie-Thérèse / Mauriello, Emilia M F / Iobbi-Nivol, Chantal

Biomolecules

2022 Volume 13, Issue 1

Abstract: Shewanella ... ...

Abstract	Shewanella oneidensis
MeSH term(s)	Bacterial Proteins/genetics ; Chemotaxis/physiology ; Shewanella/genetics
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2022-12-22
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13010021
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Article ; Online: Cellular targeting and segregation of bacterial chemosensory systems.

Mauriello, Emilia M F / Jones, Christopher / Moine, Audrey / Armitage, Judith P

FEMS microbiology reviews

2018 Volume 42, Issue 4, Page(s) 462–476

Abstract: The bacterial cytoplasm is not a homogeneous solution of macromolecules, but rather a highly organized and compartmentalized space where the clustering and segregation of macromolecular complexes in certain cell regions confers functional efficiency. ... ...

Abstract	The bacterial cytoplasm is not a homogeneous solution of macromolecules, but rather a highly organized and compartmentalized space where the clustering and segregation of macromolecular complexes in certain cell regions confers functional efficiency. Bacterial chemoreceptors represent a versatile model system to study the subcellular localization of macromolecules, as they are present in almost all motile bacterial and archaeal species, where they tend to form highly ordered arrays that occupy distinct positions in cells. The positioning of chemoreceptor clusters, as well as their segregation mechanism on cell division, varies from species to species and probably depends on cells size, environment and speed of movement. In this review, we summarize the current understanding of the architecture and the segregation mechanisms of chemoreceptors in a limited number of bacterial model systems and suggest that the pattern of chemoreceptor distribution is coupled to behavioral life-style of that species.
MeSH term(s)	Bacteria/metabolism ; Bacterial Physiological Phenomena ; Bacterial Proteins/metabolism ; Chemotaxis/physiology ; Membrane Proteins/physiology
Chemical Substances	Bacterial Proteins ; Membrane Proteins
Language	English
Publishing date	2018-06-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1093/femsre/fuy015
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Article ; Online: Cell polarity/motility in bacteria: closer to eukaryotes than expected?

Mauriello, Emilia M F

The EMBO journal

2010 Volume 29, Issue 14, Page(s) 2258–2259

MeSH term(s)	Bacterial Proteins/metabolism ; Cell Movement/physiology ; Cell Polarity ; Eukaryota/physiology ; Guanosine Triphosphate/metabolism ; Myxococcus xanthus/physiology
Chemical Substances	Bacterial Proteins ; MglA protein, Myxococcus xanthus (123211-93-8) ; Guanosine Triphosphate (86-01-1)
Language	English
Publishing date	2010-07-21
Publishing country	England
Document type	Comment ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/emboj.2010.144
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: The polar Ras-like GTPase MglA activates type IV pilus via SgmX to enable twitching motility in

Mercier, Romain / Bautista, Sarah / Delannoy, Maëlle / Gibert, Margaux / Guiseppi, Annick / Herrou, Julien / Mauriello, Emilia M F / Mignot, Tâm

Proceedings of the National Academy of Sciences of the United States of America

2020 Volume 117, Issue 45, Page(s) 28366–28373

Abstract: Type IV pili (Tfp) are highly conserved macromolecular structures that fulfill diverse cellular functions, such as adhesion to host cells, the import of extracellular DNA, kin recognition, and cell motility (twitching). Outstandingly, twitching motility ... ...

Abstract	Type IV pili (Tfp) are highly conserved macromolecular structures that fulfill diverse cellular functions, such as adhesion to host cells, the import of extracellular DNA, kin recognition, and cell motility (twitching). Outstandingly, twitching motility enables a poorly understood process by which highly coordinated groups of hundreds of cells move in cooperative manner, providing a basis for multicellular behaviors, such as biofilm formation. In the social bacteria
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Polarity/physiology ; Fimbriae, Bacterial/metabolism ; Monomeric GTP-Binding Proteins/metabolism ; Myxococcus xanthus/cytology ; Myxococcus xanthus/genetics ; Myxococcus xanthus/physiology ; Polymorphism, Single Nucleotide ; Whole Genome Sequencing
Chemical Substances	Bacterial Proteins ; MglA protein, Myxococcus xanthus (123211-93-8) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2020-10-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2002783117
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Article ; Online: A divergent CheW confers plasticity to nucleoid-associated chemosensory arrays.

Guiseppi, Annick / Vicente, Juan Jesus / Herrou, Julien / Byrne, Deborah / Barneoud, Aurelie / Moine, Audrey / Espinosa, Leon / Basse, Marie-Jeanne / Molle, Virginie / Mignot, Tâm / Roche, Philippe / Mauriello, Emilia M F

PLoS genetics

2019 Volume 15, Issue 12, Page(s) e1008533

Abstract: ... to environmental changes. The Frz chemosensory system from M. xanthus possesses two CheW-like proteins, FrzA (the core CheW ... region responsible for this interaction. FrzB, instead, acts upstream of FrzCD in the regulation of M ...

Abstract	Chemosensory systems are highly organized signaling pathways that allow bacteria to adapt to environmental changes. The Frz chemosensory system from M. xanthus possesses two CheW-like proteins, FrzA (the core CheW) and FrzB. We found that FrzB does not interact with FrzE (the cognate CheA) as it lacks the amino acid region responsible for this interaction. FrzB, instead, acts upstream of FrzCD in the regulation of M. xanthus chemotaxis behaviors and activates the Frz pathway by allowing the formation and distribution of multiple chemosensory clusters on the nucleoid. These results, together, show that the lack of the CheA-interacting region in FrzB confers new functions to this small protein.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Movement ; Chemotaxis ; Gene Expression Regulation, Bacterial ; Methyl-Accepting Chemotaxis Proteins/genetics ; Methyl-Accepting Chemotaxis Proteins/metabolism ; Myxococcus xanthus/genetics ; Myxococcus xanthus/physiology ; Operon ; Phenotype ; Signal Transduction
Chemical Substances	Bacterial Proteins ; FrzCD protein, Myxococcus xanthus ; Methyl-Accepting Chemotaxis Proteins
Language	English
Publishing date	2019-12-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1008533
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Article: Catalytic Transfer Hydrogenolysis of Lignin-Derived Aromatic Ethers Promoted by Bimetallic Pd/Ni Systems

Mauriello, Francesco / Alina M. Balu / Emilia Paone / Rafael Luque / Rosario Pietropaolo

ACS sustainable chemistry & engineering. 2018 June 04, v. 6, no. 7

2018

Abstract: Catalytic transfer hydrogenolysis (CTH) of diphenyl ether (DPE), 2-phenethyl phenyl ether (PPE), and benzyl phenyl ether (BPE)—as model molecules of α-O-4 and β-O-4 as well as 4-O-5 lignin linkages—promoted by bimetallic Pd/Ni systems is reported. Pd/Ni ( ...

Abstract	Catalytic transfer hydrogenolysis (CTH) of diphenyl ether (DPE), 2-phenethyl phenyl ether (PPE), and benzyl phenyl ether (BPE)—as model molecules of α-O-4 and β-O-4 as well as 4-O-5 lignin linkages—promoted by bimetallic Pd/Ni systems is reported. Pd/Ni (Pd loading of 3 wt %) catalysts were synthesized by using a simple and economic coprecipitation technique, and its detailed physicochemical characterization was performed by means of H2-TPR, XRD, TEM, and XPS analysis. In the presence of palladium as cometal, an almost complete conversion of DPE was reached after 90 min at a temperature of 240 °C while BPE and PPE C–O bond breaking could be achieved at milder reaction conditions. Pd/Ni bimetallic systems can be magnetically recovered and efficiently used up to eight consecutive recycling tests in the transfer hydrogenolysis of DPE. The investigated substrates were also tested using analogous Ni monometallic systems. Palladium as cometal present in the catalysts was proven to increase the C–O bond cleavage rates and decrease aromatic ring hydrogenation selectivity. The catalytic tests on all possible reaction intermediates clearly show that the hydrogenolysis cleavage in etheric C–O bond breaking was the rate-determining step under CTH conditions, while hydrogenations only take place in a successive step. Moreover, it has been demonstrated that the hydrogenation of phenol formed from CTH depends on the type of aryl groups that form the aromatic ether structure.
Keywords	catalysts ; chemical bonding ; cleavage (chemistry) ; coprecipitation ; diphenyl ethers ; hydrogenation ; lignin ; magnetism ; models ; moieties ; nickel ; palladium ; phenol ; physicochemical properties ; recycling ; temperature ; transmission electron microscopy ; X-ray diffraction ; X-ray photoelectron spectroscopy
Language	English
Dates of publication	2018-0604
Size	p. 9269-9276.
Publishing place	American Chemical Society
Document type	Article
ISSN	2168-0485
DOI	10.1021/acssuschemeng.8b01593
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Article ; Online: AglZ regulates adventurous (A-) motility in Myxococcus xanthus through its interaction with the cytoplasmic receptor, FrzCD.

Mauriello, Emilia M F / Nan, Beiyan / Zusman, David R

Molecular microbiology

2009 Volume 72, Issue 4, Page(s) 964–977

Abstract: Myxococcus xanthus moves by gliding motility powered by type IV pili (S-motility) and distributed motor complexes (A-motility). The Frz chemosensory pathway controls reversals for both motility systems. However, it is unclear how the Frz pathway can ... ...

Abstract	Myxococcus xanthus moves by gliding motility powered by type IV pili (S-motility) and distributed motor complexes (A-motility). The Frz chemosensory pathway controls reversals for both motility systems. However, it is unclear how the Frz pathway can communicate with these different systems. In this article, we show that FrzCD, the Frz pathway receptor, interacts with AglZ, a protein associated with A-motility. Affinity chromatography and cross-linking experiments showed that the FrzCD-AglZ interaction occurs between the uncharacterized N-terminal region of FrzCD and the N-terminal pseudo-receiver domain of AglZ. Fluorescence microscopy showed AglZ-mCherry and FrzCD-GFP localized in clusters that occupy different positions in cells. To study the role of the Frz system in the regulation of A-motility, we constructed aglZ frzCD double mutants and aglZ frzCD pilA triple mutants. To our surprise, these mutants, predicted to show no A-motility (A-S+) or no motility at all (A-S-), respectively, showed restored A-motility. These results indicate that AglZ modulates a FrzCD activity that inhibits A-motility. We hypothesize that AglZ-FrzCD interactions are favoured when cells are isolated and moving by A-motility and inhibited when S-motility predominates and A-motility is reduced.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Movement ; Mutagenesis ; Myxococcus xanthus/cytology ; Myxococcus xanthus/genetics ; Myxococcus xanthus/metabolism ; Protein Interaction Domains and Motifs
Chemical Substances	Bacterial Proteins ; FrzCD protein, Myxococcus xanthus
Language	English
Publishing date	2009-04-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/j.1365-2958.2009.06697.x
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