Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome.

Pistocchi, Rossella; Kashiwagi, Keiko; Miyamoto, Saku; Nukui, Eiji; Sadakata, Y; Kobayashi, Hiroshi; Igarashi, Kazuei

doi:10.1016/s0021-9258(18)54126-0

Cited by 106 publications

(27 citation statements)

References 46 publications

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“…Almost all bacteria can also import extracellular polyamines by a polyamine ATP-binding cassette (ABC) transporter, encoded by an operon of four genes [4,20,21]. Some bacteria, such as E. coli, possess two polyamine ABC transporters, PotABCD and PotFGHI, having a higher affinity for either spermidine or putrescine, respectively [22,23]. Only a single potABCD operon is detected in many other bacteria, such as Staphylococcus aureus, S. pneumoniae, S. suis or Streptococcus agalactiae [19,[24][25][26][27].…”

Section: Introductionmentioning

confidence: 99%

“…PotB with PotC or PotH with PotI constitute transmembrane channels for polyamine transport. Located in the periplasm or anchored to the cytoplasmic membrane, PotD and PotF are substrate-binding proteins that trap extracellular polyamines [22,23]. The binding of polyamine to the substratebinding proteins results in a conformational change of the membrane spanning proteins of the transporter, which leads to ATP hydrolysis and polyamine uptake.…”

Section: Introductionmentioning

confidence: 99%

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Investigation of the polyamine biosynthetic and transport capability of Streptococcus agalactiae: the non-essential PotABCD transporter

et al. 2021

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Polyamines constitute a group of organic polycations positively charged at physiological pH. They are involved in a large variety of biological processes, including the protection against physiological stress. In this study, we show that the genome of Streptococcus agalactiae , a commensal bacterium of the intestine and the vagina and one of the most common agents responsible of neonate infections, does not encode proteins homologous to the specific enzymes involved in the known polyamine synthetic pathways. This lack of biosynthetic capability was verified experimentally by TLC analysis of the intracellular content of S. agalactiae grown in the absence of polyamines. However, similar analyses showed that the polyamines spermidine, spermine and putrescine can be imported from the growth media into the bacteria. We found that all strains of S. agalactiae possess the genes encoding the polyamine ABC transporter PotABCD. We demonstrated that these genes form an operon with folK, a gene involved in folate biosynthesis, murB, a gene involved in peptidoglycan biosynthesis, and with clc, a gene encoding a Cl−/H+ antiporter involved in resistance to acid stress in Escherichia coli . Transcription of the potABCD operon is induced by peroxide-induced oxidative stress but not by acidic stress. Spermidine and spermine were found to be inducers of potABCD transcription at pH 7.4 whereas putrescine induces this expression only during peroxide-induced oxidative stress. Using a deletion mutant of potABCD, we were nevertheless unable to associate phenotypic traits to the PotABCD transporter, probably due to the existence of one or more as yet identified transporters with a redundant action.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Investigation of the polyamine biosynthetic and transport capability of Streptococcus agalactiae: the non-essential PotABCD transporter

et al. 2021

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“…Although microorganisms can obtain polyamines through the subtle multiple de novo synthesis pathways, the cost-effective transport systems, such as PotABCD, or other putrescine-specific transporter systems PotF, PotH, PotI and PotG in E. coli, still occupy essential parts in polyamine accumulation [Furuchi et al, 1991]. These conclusions have been drawn from the observation of the construction of ΔpotD and its polyamineuptake capacity alteration using the radiolabeled polyamines through rapid filtration method [Pistocchi et al, 1993;Raksajit et al, 2006]. The removal of one transport element could significantly decrease the pool of available polyamines, or at least, possibly make the selfsynthesis pathway engage as a compensatory supplement for a certain kind of polyamine, which may happen at the cost of energy consumption that brings about energy depletion of other pathways as a whole.…”

Section: Discussionmentioning

confidence: 99%

Deletion of Polyamine Transport Protein PotD Exacerbates Virulence in Glaesserella (Haemophilus) parasuis in the Form of Non-biofilm-generated Bacteria in a Murine Acute Infection Model

Dai

Yang

et al. 2021

Virulence

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Polyamines are small, polycationic molecules with a hydrocarbon backbone and multiple amino groups required for optimal cell growth. The potD gene, belonging to the ABC (ATP-binding cassette) transport system potABCD, encodes the bacterial substrate-binding subunit of the polyamine transport system, playing a pivotal role in bacterial metabolism and growth. The swine pathogen Glaesserella parasuis possesses an intact pot operon, and the studies presented here mainly examined the involvement of PotD in Glaesserella pathogenesis. A potD-deficient mutant was constructed using a virulent G. parasuis strain SC1401 by natural transformation; immuno-electron microscopy was used to identify the subcellular location of native PotD protein; an electron microscope was adopted to inspect biofilm and bacterial morphology; immunofluorescence technique was employed to study cellular adhesion, the levels of inflammation and apoptosis. The TSA++-pre-cultured mutant strain showed a significantly reduced adhesion capacity to PK-15 and MLE-12 cells. Likewise, we also found attenuation in virulence using murine models focusing on the clinical sign, H&E, and IFA for inflammation and apoptosis. However, when the mutant was grown in TSB++, virulence recovered to normal levels, along with a high level of radical oxygen species formation in the host. The expression of PotD could actively stimulate the production of ROS in Raw 264.7. Our data suggested that PotD from G. parasuis has a high binding potential to polyamine, and is essential for the full bacterial virulence within mouse models. However, the virulence of the potD mutant is highly dependent on its TSA++ culture conditions rather than on biofilm-formation.

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“…Because of the cationic function of polyamine, it cannot penetrate through the cell membrane. Two spermidine transporters, PotABCD and MdtJI, and six putrescine transporters, PuuP, YdcSTUV, PlaP, PotE, PotFGHI, and SapBCDF, have been identified (Kashiwagi et al 1992 ; Pistocchi et al 1993 ; Kurihara et al 2009a , b ; Kurihara et al 2011 ; Saier et al 2016 ; Sugiyama et al 2016 ). We recently reported that PotFGHI can import spermidine under biofilm-forming conditions (Thongbhubate et al 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Improvement of putrescine production through the arginine decarboxylase pathway in Escherichia coli K-12

et al. 2021

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In the bio-based polymer industry, putrescine is in the spotlight for use as a material. We constructed strains of Escherichia coli to assess its putrescine production capabilities through the arginine decarboxylase pathway in batch fermentation. N-Acetylglutamate (ArgA) synthase is subjected to feedback inhibition by arginine. Therefore, the 19th amino acid residue, Tyr, of argA was substituted with Cys to desensitize the feedback inhibition of arginine, resulting in improved putrescine production. The inefficient initiation codon GTG of argA was substituted with the effective ATG codon, but its replacement did not affect putrescine production. The essential genes for the putrescine production pathway, speA and speB, were cloned into the same plasmid with argAATG Y19C to form an operon. These genes were introduced under different promoters; lacIp, lacIqp, lacIq1p, and T5p. Among these, the T5 promoter demonstrated the best putrescine production. In addition, disruption of the puuA gene encoding enzyme of the first step of putrescine degradation pathway increased the putrescine production. Of note, putrescine production was not affected by the disruption of patA, which encodes putrescine aminotransferase, the initial enzyme of another putrescine utilization pathway. We also report that the strain KT160, which has a genomic mutation of YifEQ100TAG, had the greatest putrescine production. At 48 h of batch fermentation, strain KT160 grown in terrific broth with 0.01 mM IPTG produced 19.8 mM of putrescine.

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Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome.

Cited by 106 publications

References 46 publications

Investigation of the polyamine biosynthetic and transport capability of Streptococcus agalactiae: the non-essential PotABCD transporter

Investigation of the polyamine biosynthetic and transport capability of Streptococcus agalactiae: the non-essential PotABCD transporter

Deletion of Polyamine Transport Protein PotD Exacerbates Virulence in Glaesserella (Haemophilus) parasuis in the Form of Non-biofilm-generated Bacteria in a Murine Acute Infection Model

Improvement of putrescine production through the arginine decarboxylase pathway in Escherichia coli K-12

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