A critical phosphate concentration in the stationary phase maintainsndhgene expression and aerobic respiratory chain activity inEscherichia coli

Schurig-Briccio, Lici A.; Rintoul, María R.; Volentini, Sabrina Inès; Farı́as, Ricardo N.; Baldomà, Laura; Badı́a, Josefa; Rodrı́guez-Montelongo, Luisa; Rapisarda, Viviana Andrea

doi:10.1111/j.1574-6968.2008.01188.x

Cited by 16 publications

(22 citation statements)

References 29 publications

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“…In contrast, it has been demonstrated in our laboratory that, in media containing high Pi concentration (>25-37 mM), E. coli cells maintained the polyP pool during the stationary phase (Scrurig-Briccio et al, 2009b;Grillo-Puertas et al, 2012). This maintenance of polyP levels has been related to the maintenance of the expression of aerobic respiratory chain genes, protection against oxidative stress and inhibition of biofilm formation (Schurig-Briccio et al, 2008, 2009aGrillo-Puertas et al, 2012. Actually, to trigger biofilm formation, not only the presence of polyP but also its degradation is required (Grillo-Puertas et al, 2012.…”

Section: Introductionmentioning

confidence: 83%

PhoB activation in non-limiting phosphate condition by the maintenance of high polyphosphate levels in the stationary phase inhibits biofilm formation in Escherichia coli

2016

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Polyphosphate (polyP) degradation in Escherichia coli stationary phase triggers biofilm formation via the LuxS quorum sensing system. In media containing excess of phosphate (Pi), high polyP levels are maintained in the stationary phase with the consequent inhibition of biofilm formation. The transcriptional-response regulator PhoB, which is activated under Pi limitation, is involved in the inhibition of biofilm formation in several bacterial species. In the current study, we report, for the first time, we believe that E. coli PhoB can be activated in non-limiting Pi conditions, leading to inhibition of biofilm formation. In fact, PhoB was activated when high polyP levels were maintained in the stationary phase, whereas it remained inactive when the polymer was degraded or absent. PhoB activation was mediated by acetyl phosphate with the consequent repression of biofilm formation owing to the downregulation of c-di-GMP synthesis and the inhibition of autoinducer-2 production. These results allowed us to propose a model showing that PhoB is a component in the signal cascade regulating biofilm formation triggered by fluctuations of polyP levels in E. coli cells during stationary phase.

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Section: Introductionmentioning

confidence: 83%

PhoB activation in non-limiting phosphate condition by the maintenance of high polyphosphate levels in the stationary phase inhibits biofilm formation in Escherichia coli

2016

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“…Following hydrolysis of polyP to Pi, the metal/Pi complexes would be exported through the Pit transporters. PolyP is also involved in cell signaling, respiratory chain gene expression, bacterial persistence, and in stress response networks [93][94][95][96]. It has recently been shown that when external Pi levels are very high, polyP can even activate PhoB during the stati o n a r yp h a s eo fg r o w t ht h r o u g ht h es m a l l molecule acetyl phosphate [97].…”

Section: The Response To High Levels Of Extracellular Pimentioning

confidence: 99%

Molecular Mechanisms of Phosphate Homeostasis in Escherichia coli

McCleary¹

2017

≪i>Escherichia Coli

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Life's processes absolutely require inorganic phosphate for structural and energetic purposes. Escherichia coli has developed sophisticated mechanisms to acquire phosphate and to maintain intracellular amounts at optimal levels. The processes by which these simple cells maintain stable intracellular concentrations of phosphate are termed phosphate homeostasis, which involves mechanisms to balance the import, assimilation, sequestration, and export of phosphate. This chapter introduces the proteins involved in phosphate homeostasis and reviews information concerning the multiple phosphate transporters and the mechanisms by which they are regulated. It also introduces new concepts of how this bacterium responds to elevated extracellular levels of phosphate and presents a model for the integration of all of these processes to achieve homeostasis. The predominant importers are PitA, PitB, and the PstSCAB complex. Assimilation, or the incorporation of Pi into organic molecules, occurs primarily through the formation of ATP. Gene regulation relies on the PhoB/PhoR two-component system and the formation of a signaling complex at the membrane. The amount of intracellular phosphate can be fine-tuned through the formation or degradation of polyphosphate. Polyphosphate formation requires adequate supplies of ATP. In addition, when intracellular phosphate levels become too high, phosphate can be exported through PitA, PitB, or the YjbB transporters.

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“…The O2 consumption rates were measured with a Clark-type O2 electrode in 2-ml stirred sample chambers at 37°C, as described by Schurig-Briccio et al (34). The adipocytes were harvested by trypsinization and resuspended in DMEM containing 10% calf serum, at which point the cells in the suspensions were counted in a hemocytometer (2.0 ϫ 10 6 cells/ml).…”

Section: Chemicals and Antibodiesmentioning
confidence: 99%

Role of bone morphogenetic protein 4 in the differentiation of brown fat-like adipocytes
Xue
¹
,
Wan
²
,
Zhang
³

et al. 2014
American Journal of Physiology-Endocrinology and Metabolism
66
2
49
1
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There are two different types of fat present in mammals: white adipose tissue, the primary site of energy storage, and brown adipose tissue, which is specializes in energy expenditure. Factors that specify the developmental fate and function of brown fat are poorly understood. Bone morphogenic proteins (BMPs) play an important role in adipogenesis. While BMP4 is capable of triggering commitment of stem cells to the white adipocyte lineage, BMP7 triggers commitment of progenitor cells to a brown adipocyte lineage and activates brown adipogenesis. To investigate the differential effects of BMPs on the development of adipocytes, C3H10T1/2 pluripotent cells were pretreated with BMP4 and BMP7, followed by different adipogenic induction cocktails. Both BMP4 and BMP7 unexpectedly activated a full program of brown adipogenesis, including induction of the brown fat-defining marker uncoupling protein-1 (UCP1), increasing the expression of early regulators of brown fat fate PRDM16 (PR domain-containing 16) and induction of mitochondrial biogenesis and function. Implantation of BMP4-pretreated C3H10T1/2 cells into nude mice resulted in the development of adipose tissue depots containing UCP1-positive brown adipocytes. Interestingly, BMP4 could also induce brown fat-like adipocytes in both white and brown preadipocytes, thereby decreasing the classical brown adipocyte marker Zic1 and increasing the recently identified beige adipocyte marker TMEM26. The data indicate an important role for BMP4 in promoting brown adipocyte differentiation and thermogenesis in vivo and in vitro and offers a potentially new therapeutic approach for the treatment of obesity.

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A critical phosphate concentration in the stationary phase maintainsndhgene expression and aerobic respiratory chain activity inEscherichia coli

Cited by 16 publications

References 29 publications

PhoB activation in non-limiting phosphate condition by the maintenance of high polyphosphate levels in the stationary phase inhibits biofilm formation in Escherichia coli

PhoB activation in non-limiting phosphate condition by the maintenance of high polyphosphate levels in the stationary phase inhibits biofilm formation in Escherichia coli

Molecular Mechanisms of Phosphate Homeostasis in <i>Escherichia coli</i>

Role of bone morphogenetic protein 4 in the differentiation of brown fat-like adipocytes

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