Novel (p)ppGpp Binding and Metabolizing Proteins of Escherichia coli

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00490330" target="_blank" >RIV/61388963:_____/18:00490330 - isvavai.cz</a>

Výsledek na webu

<a href="http://mbio.asm.org/content/9/2/e02188-17.full" target="_blank" >http://mbio.asm.org/content/9/2/e02188-17.full</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/mBio.02188-17" target="_blank" >10.1128/mBio.02188-17</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Novel (p)ppGpp Binding and Metabolizing Proteins of Escherichia coli

Popis výsledku v původním jazyce

The alarmone (p) ppGpp plays pivotal roles in basic bacterial stress responses by increasing tolerance of various nutritional limitations and chemical insults, including antibiotics. Despite intensive studies since (p) ppGpp was discovered over 4 decades ago, (p) ppGpp binding proteins have not been systematically identified in Escherichia coli. We applied DRaCALA (differential radial capillary action of ligand assay) to identify (p) ppGpp-protein interactions. We discovered 12 new (p) ppGpp targets in E. coli that, based on their physiological functions, could be classified into four major groups, involved in (i) purine nucleotide homeostasis (YgdH), (ii) ribosome biogenesis and translation (RsgA, Era, HflX, and LepA), (iii) maturation of dehydrogenases (HypB), and (iv) metabolism of (p) ppGpp (MutT, NudG, TrmE, NadR, PhoA, and UshA). We present a comprehensive and comparative biochemical and physiological characterization of these novel (p) ppGpp targets together with a comparative analysis of relevant, known (p) ppGpp binding proteins. Via this, primary targets of (p) ppGpp in E. coli are identified. The GTP salvage biosynthesis pathway and ribosome biogenesis and translation are confirmed as targets of (p) ppGpp that are highly conserved between E. coli and Firmicutes. In addition, an alternative (p) ppGpp degradative pathway, involving NudG and MutT, was uncovered. This report thus significantly expands the known cohort of (p) ppGpp targets in E. coli.

Název v anglickém jazyce

Novel (p)ppGpp Binding and Metabolizing Proteins of Escherichia coli

Popis výsledku anglicky

The alarmone (p) ppGpp plays pivotal roles in basic bacterial stress responses by increasing tolerance of various nutritional limitations and chemical insults, including antibiotics. Despite intensive studies since (p) ppGpp was discovered over 4 decades ago, (p) ppGpp binding proteins have not been systematically identified in Escherichia coli. We applied DRaCALA (differential radial capillary action of ligand assay) to identify (p) ppGpp-protein interactions. We discovered 12 new (p) ppGpp targets in E. coli that, based on their physiological functions, could be classified into four major groups, involved in (i) purine nucleotide homeostasis (YgdH), (ii) ribosome biogenesis and translation (RsgA, Era, HflX, and LepA), (iii) maturation of dehydrogenases (HypB), and (iv) metabolism of (p) ppGpp (MutT, NudG, TrmE, NadR, PhoA, and UshA). We present a comprehensive and comparative biochemical and physiological characterization of these novel (p) ppGpp targets together with a comparative analysis of relevant, known (p) ppGpp binding proteins. Via this, primary targets of (p) ppGpp in E. coli are identified. The GTP salvage biosynthesis pathway and ribosome biogenesis and translation are confirmed as targets of (p) ppGpp that are highly conserved between E. coli and Firmicutes. In addition, an alternative (p) ppGpp degradative pathway, involving NudG and MutT, was uncovered. This report thus significantly expands the known cohort of (p) ppGpp targets in E. coli.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA15-11711S" target="_blank" >GA15-11711S: Vývoj molekulárních nástrojů pro ovlivňování a výzkum bakteriální stringentní odpovědi</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

mBio

ISSN

2150-7511

e-ISSN

—

Svazek periodika

9

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

20

Strana od-do

—

Kód UT WoS článku

000431279600021

EID výsledku v databázi Scopus

2-s2.0-85046494288