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Artikel ; Online: The YmgB-SpoT interaction triggers the stringent response in Escherichia coli.

Guiraud, Paul / Germain, Elsa / Byrne, Deborah / Maisonneuve, Etienne

2023 Band 299, Heft 12, Seite(n) 105429

Abstract: Virtually all bacterial species synthesize (p)ppGpp (guanosine penta- or tetraphosphate), a pleiotropic regulator of the so-called stringent response, which controls many aspects of cellular physiology and metabolism. In Escherichia coli, (p)ppGpp levels ...

Abstract	Virtually all bacterial species synthesize (p)ppGpp (guanosine penta- or tetraphosphate), a pleiotropic regulator of the so-called stringent response, which controls many aspects of cellular physiology and metabolism. In Escherichia coli, (p)ppGpp levels are controlled by two homologous enzymes: the (p)ppGpp synthetase RelA and the bifunctional synthetase/hydrolase SpoT. We recently identified several protein candidates that can modulate (p)ppGpp levels in E. coli. In this work, we show that the putative two-component system connector protein YmgB can promote SpoT-dependent accumulation of ppGpp in E. coli. Importantly, we determined that the control of SpoT activities by YmgB is independent of its proposed role in the two-component Rcs system, and these two functions can be uncoupled. Using genetic and structure-function analysis, we show that the regulation of SpoT activities by YmgB occurs by functional and direct binding in vivo and in vitro to the TGS and Helical domains of SpoT. These results further support the role of these domains in controlling the reciprocal enzymatic states.
Mesh-Begriff(e)	Escherichia coli/metabolism ; Guanosine Pentaphosphate/genetics ; Bacteria/metabolism ; Guanosine Tetraphosphate ; Hydrolases/metabolism ; Ligases/genetics ; Ligases/metabolism ; Gene Expression Regulation, Bacterial ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism
Chemische Substanzen	Guanosine Pentaphosphate (38918-96-6) ; Guanosine Tetraphosphate (33503-72-9) ; Hydrolases (EC 3.-) ; Ligases (EC 6.-) ; YmgB protein, E coli ; Escherichia coli Proteins
Sprache	Englisch
Erscheinungsdatum	2023-11-04
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105429
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Regulation of

Meyer, Laura / Germain, Elsa / Maisonneuve, Etienne

Frontiers in microbiology

2021 Band 12, Seite(n) 775164

Abstract: Guanosine penta- or tetraphosphate (known as (p)ppGpp) serves as second messenger to respond to nutrient downshift and other environmental stresses, a phenomenon called stringent response. Accumulation of (p)ppGpp promotes the coordinated inhibition of ... ...

Abstract	Guanosine penta- or tetraphosphate (known as (p)ppGpp) serves as second messenger to respond to nutrient downshift and other environmental stresses, a phenomenon called stringent response. Accumulation of (p)ppGpp promotes the coordinated inhibition of macromolecule synthesis, as well as the activation of stress response pathways to cope and adapt to harmful conditions. In
Sprache	Englisch
Erscheinungsdatum	2021-11-04
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.775164
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: NirD curtails the stringent response by inhibiting RelA activity in

Léger, Loïc / Byrne, Deborah / Guiraud, Paul / Germain, Elsa / Maisonneuve, Etienne

eLife

2021 Band 10

Abstract: Bacteria regulate their metabolism to adapt and survive adverse conditions, in particular to stressful downshifts in nutrient availability. These shifts trigger the so-called stringent response, coordinated by the signaling molecules guanosine tetra and ... ...

Abstract	Bacteria regulate their metabolism to adapt and survive adverse conditions, in particular to stressful downshifts in nutrient availability. These shifts trigger the so-called stringent response, coordinated by the signaling molecules guanosine tetra and pentaphosphate collectively referred to as (p)ppGpp. In
Mesh-Begriff(e)	Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; GTP Pyrophosphokinase/genetics ; GTP Pyrophosphokinase/metabolism ; Guanosine Pentaphosphate/metabolism ; Nitrite Reductases/genetics ; Nitrite Reductases/metabolism ; Stress, Physiological
Chemische Substanzen	Escherichia coli Proteins ; Guanosine Pentaphosphate (38918-96-6) ; Nitrite Reductases (EC 1.7.-) ; GTP Pyrophosphokinase (EC 2.7.6.5) ; relA protein, E coli (EC 2.7.6.5)
Sprache	Englisch
Erscheinungsdatum	2021-07-29
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.64092
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: YtfK activates the stringent response by triggering the alarmone synthetase SpoT in Escherichia coli.

Germain, Elsa / Guiraud, Paul / Byrne, Deborah / Douzi, Badreddine / Djendli, Meriem / Maisonneuve, Etienne

Nature communications

2019 Band 10, Heft 1, Seite(n) 5763

Abstract: The stringent response is a general bacterial stress response that allows bacteria to adapt and survive adverse conditions. This reprogramming of cell physiology is caused by the accumulation of the alarmone (p)ppGpp which, in Escherichia coli, depends ... ...

Abstract	The stringent response is a general bacterial stress response that allows bacteria to adapt and survive adverse conditions. This reprogramming of cell physiology is caused by the accumulation of the alarmone (p)ppGpp which, in Escherichia coli, depends on the (p)ppGpp synthetase RelA and the bifunctional (p)ppGpp synthetase/hydrolase SpoT. Although conditions that control SpoT-dependent (p)ppGpp accumulation have been described, the molecular mechanisms regulating the switching from (p)ppGpp degradation to synthesis remain poorly understood. Here, we show that the protein YtfK promotes SpoT-dependent accumulation of (p)ppGpp in E. coli and is required for activation of the stringent response during phosphate and fatty acid starvation. Our results indicate that YtfK can interact with SpoT. We propose that YtfK activates the stringent response by tilting the catalytic balance of SpoT toward (p)ppGpp synthesis.
Mesh-Begriff(e)	Escherichia coli/physiology ; Escherichia coli Proteins/metabolism ; Guanosine Pentaphosphate/biosynthesis ; Pyrophosphatases/metabolism ; Stress, Physiological
Chemische Substanzen	Escherichia coli Proteins ; ytfK protein, E coli ; Guanosine Pentaphosphate (38918-96-6) ; guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase (EC 3.1.7.2) ; Pyrophosphatases (EC 3.6.1.-)
Sprache	Englisch
Erscheinungsdatum	2019-12-17
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-13764-4
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Peptide-nucleotide antibiotic Microcin C is a potent inducer of stringent response and persistence in both sensitive and producing cells.

Piskunova, Julia / Maisonneuve, Etienne / Germain, Elsa / Gerdes, Kenn / Severinov, Konstantin

Molecular microbiology

2017 Band 104, Heft 3, Seite(n) 463–471

Abstract: Microcin C (McC) is a peptide-nucleotide antibiotic that inhibits aspartyl-tRNA synthetase. Here, we show that McC is a strong inducer of persistence in Escherichia coli. Persistence induced by McC is mediated by (p)ppGpp and requires chromosomally ... ...

Abstract	Microcin C (McC) is a peptide-nucleotide antibiotic that inhibits aspartyl-tRNA synthetase. Here, we show that McC is a strong inducer of persistence in Escherichia coli. Persistence induced by McC is mediated by (p)ppGpp and requires chromosomally encoded toxin-antitoxin modules. McC-producing cells have increased persistence levels due to a combined effect of McC imported from the cultured medium and intracellularly synthesized antibiotic. McC-producing cells also induce persistence in sensitive cells during co-cultivation, underscoring complex interactions in bacterial communities where an antagonistic compound produced by one community member can benefit other members by increasing their ability to withstand antibiotics.
Mesh-Begriff(e)	Anti-Bacterial Agents/pharmacology ; Aspartate-tRNA Ligase/metabolism ; Bacteriocins/pharmacology ; Escherichia coli/drug effects ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial/drug effects ; Phosphorylation
Chemische Substanzen	Anti-Bacterial Agents ; Bacteriocins ; Escherichia coli Proteins ; microcin (1403-96-9) ; Aspartate-tRNA Ligase (EC 6.1.1.12)
Sprache	Englisch
Erscheinungsdatum	2017-02-24
Erscheinungsland	England
Dokumenttyp	Journal Article
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.13640
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Stochastic induction of persister cells by HipA through (p)ppGpp-mediated activation of mRNA endonucleases.

Germain, Elsa / Roghanian, Mohammad / Gerdes, Kenn / Maisonneuve, Etienne

Publikation ZURÜCKGEZOGEN

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

2015 Band 112, Heft 16, Seite(n) 5171–5176

Abstract: The model organism Escherichia coli codes for at least 11 type II toxin-antitoxin (TA) modules, all implicated in bacterial persistence (multidrug tolerance). Ten of these encode messenger RNA endonucleases (mRNases) inhibiting translation by catalytic ... ...

Abstract	The model organism Escherichia coli codes for at least 11 type II toxin-antitoxin (TA) modules, all implicated in bacterial persistence (multidrug tolerance). Ten of these encode messenger RNA endonucleases (mRNases) inhibiting translation by catalytic degradation of mRNA, and the 11th module, hipBA, encodes HipA (high persister protein A) kinase, which inhibits glutamyl tRNA synthetase (GltX). In turn, inhibition of GltX inhibits translation and induces the stringent response and persistence. Previously, we presented strong support for a model proposing (p)ppGpp (guanosine tetra and penta-phosphate) as the master regulator of persistence. Stochastic variation of [(p)ppGpp] in single cells induced TA-encoded mRNases via a pathway involving polyphosphate and Lon protease. Polyphosphate activated Lon to degrade all known type II antitoxins of E. coli. In turn, the activated mRNases induced persistence and multidrug tolerance. However, even though it was known that activation of HipA stimulated (p)ppGpp synthesis, our model did not explain how hipBA induced persistence. Here we show that, in support of and consistent with our initial model, HipA-induced persistence depends not only on (p)ppGpp but also on the 10 mRNase-encoding TA modules, Lon protease, and polyphosphate. Importantly, observations with single cells convincingly show that the high level of (p)ppGpp caused by activation of HipA does not induce persistence in the absence of TA-encoded mRNases. Thus, slow growth per se does not induce persistence in the absence of TA-encoded toxins, placing these genes as central effectors of bacterial persistence.
Mesh-Begriff(e)	Alleles ; Antitoxins/metabolism ; Bacterial Toxins/metabolism ; Endonucleases/metabolism ; Enzyme Activation ; Escherichia coli Proteins/metabolism ; Guanosine Pentaphosphate/metabolism ; Guanosine Tetraphosphate/metabolism ; Models, Molecular ; RNA, Messenger/metabolism ; Stochastic Processes ; Time-Lapse Imaging
Chemische Substanzen	Antitoxins ; Bacterial Toxins ; Escherichia coli Proteins ; RNA, Messenger ; hipA protein, E coli (144515-93-5) ; Guanosine Tetraphosphate (33503-72-9) ; Guanosine Pentaphosphate (38918-96-6) ; Endonucleases (EC 3.1.-)
Sprache	Englisch
Erscheinungsdatum	2015-04-06
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Retracted Publication
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1423536112
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: HipA-Mediated Phosphorylation of SeqA Does not Affect Replication Initiation in

Riber, Leise / Koch, Birgit M / Kruse, Line Riis / Germain, Elsa / Løbner-Olesen, Anders

Frontiers in microbiology

2018 Band 9, Seite(n) 2637

Abstract: The SeqA protein ... ...

Abstract	The SeqA protein of
Sprache	Englisch
Erscheinungsdatum	2018-11-02
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2018.02637
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: The kinases HipA and HipA7 phosphorylate different substrate pools in

Semanjski, Maja / Germain, Elsa / Bratl, Katrin / Kiessling, Andreas / Gerdes, Kenn / Macek, Boris

Science signaling

2018 Band 11, Heft 547

Abstract: The bacterial serine-threonine protein kinase HipA promotes multidrug tolerance by phosphorylating the glutamate-tRNA ligase (GltX), leading to a halt in translation, inhibition of growth, and induction of a physiologically dormant state (persistence). ... ...

Abstract	The bacterial serine-threonine protein kinase HipA promotes multidrug tolerance by phosphorylating the glutamate-tRNA ligase (GltX), leading to a halt in translation, inhibition of growth, and induction of a physiologically dormant state (persistence). The HipA variant HipA7 substantially increases persistence despite being less efficient at inhibiting cell growth. We postulated that this phenotypic difference was caused by differences in the substrates targeted by both kinases. We overproduced HipA and HipA7 in
Mesh-Begriff(e)	DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Drug Tolerance ; Escherichia coli/genetics ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Glutamate-tRNA Ligase/genetics ; Glutamate-tRNA Ligase/metabolism ; Phosphorylation ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Signal Transduction/genetics ; Substrate Specificity
Chemische Substanzen	DNA-Binding Proteins ; Escherichia coli Proteins ; Protein Isoforms ; hipB protein, E coli (144515-91-3) ; hipA protein, E coli (144515-93-5) ; Glutamate-tRNA Ligase (EC 6.1.1.17)
Sprache	Englisch
Erscheinungsdatum	2018-09-11
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.aat5750
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Proteome Dynamics during Antibiotic Persistence and Resuscitation.

Semanjski, Maja / Gratani, Fabio Lino / Englert, Till / Nashier, Payal / Beke, Viktor / Nalpas, Nicolas / Germain, Elsa / George, Shilpa / Wolz, Christiane / Gerdes, Kenn / Macek, Boris

mSystems

2021 Band 6, Heft 4, Seite(n) e0054921

Abstract: During antibiotic persistence, bacterial cells become transiently tolerant to antibiotics by restraining their growth and metabolic activity. Detailed molecular characterization of antibiotic persistence is hindered by low count of persisting cells and ... ...

Abstract	During antibiotic persistence, bacterial cells become transiently tolerant to antibiotics by restraining their growth and metabolic activity. Detailed molecular characterization of antibiotic persistence is hindered by low count of persisting cells and the need for their isolation. Here, we used sustained addition of stable isotope-labeled lysine to selectively label the proteome during
Sprache	Englisch
Erscheinungsdatum	2021-08-24
Erscheinungsland	United States
Dokumenttyp	Journal Article
ISSN	2379-5077
ISSN	2379-5077
DOI	10.1128/mSystems.00549-21
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Molecular mechanism of bacterial persistence by HipA.

Germain, Elsa / Castro-Roa, Daniel / Zenkin, Nikolay / Gerdes, Kenn

Molecular cell

2013 Band 52, Heft 2, Seite(n) 248–254

Abstract: HipA of Escherichia coli is a eukaryote-like serine-threonine kinase that inhibits cell growth and induces persistence (multidrug tolerance). Previously, it was proposed that HipA inhibits cell growth by the phosphorylation of the essential translation ... ...

Abstract	HipA of Escherichia coli is a eukaryote-like serine-threonine kinase that inhibits cell growth and induces persistence (multidrug tolerance). Previously, it was proposed that HipA inhibits cell growth by the phosphorylation of the essential translation factor EF-Tu. Here, we provide evidence that EF-Tu is not a target of HipA. Instead, a genetic screen reveals that the overexpression of glutamyl-tRNA synthetase (GltX) suppresses the toxicity of HipA. We show that HipA phosphorylates conserved Ser(239) near the active center of GltX and inhibits aminoacylation, a unique example of an aminoacyl-tRNA synthetase being inhibited by a toxin encoded by a toxin-antitoxin locus. HipA only phosphorylates tRNA(Glu)-bound GltX, which is consistent with the earlier finding that the regulatory motif containing Ser(239) changes configuration upon tRNA binding. These results indicate that HipA mediates persistence by the generation of "hungry" codons at the ribosomal A site that trigger the synthesis of (p)ppGpp, a hypothesis that we verify experimentally.
Mesh-Begriff(e)	Adenosine Triphosphate/metabolism ; Aminoacylation ; Anti-Bacterial Agents/pharmacology ; Binding Sites/genetics ; Drug Tolerance ; Escherichia coli/drug effects ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Glutamate-tRNA Ligase/chemistry ; Glutamate-tRNA Ligase/genetics ; Glutamate-tRNA Ligase/metabolism ; Guanosine Pentaphosphate/metabolism ; Models, Genetic ; Models, Molecular ; Mutation ; Peptide Elongation Factor Tu/genetics ; Peptide Elongation Factor Tu/metabolism ; Phosphorylation ; Protein Biosynthesis ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Protein Structure, Tertiary ; RNA, Transfer, Glu/genetics ; RNA, Transfer, Glu/metabolism ; Ribosomes/genetics ; Ribosomes/metabolism ; Serine/chemistry ; Serine/genetics ; Serine/metabolism
Chemische Substanzen	Anti-Bacterial Agents ; Escherichia coli Proteins ; RNA, Transfer, Glu ; hipA protein, E coli (144515-93-5) ; Guanosine Pentaphosphate (38918-96-6) ; Serine (452VLY9402) ; Adenosine Triphosphate (8L70Q75FXE) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Peptide Elongation Factor Tu (EC 3.6.1.-) ; Glutamate-tRNA Ligase (EC 6.1.1.17)
Sprache	Englisch
Erscheinungsdatum	2013-10-03
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2013.08.045
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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