Identification of a Meningococcal L-glutamate ABC Transporter operon essential for growth in low-sodium environments (Articolo in rivista)

Type
Label
  • Identification of a Meningococcal L-glutamate ABC Transporter operon essential for growth in low-sodium environments (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Alternative label
  • Monaco C, Tala A, Spinosa MR, Progida C, De Nitto E, Gaballo A, Bruni CB, Bucci C, Alifano P. (2006)
    Identification of a Meningococcal L-glutamate ABC Transporter operon essential for growth in low-sodium environments
    in Infection and immunity (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Monaco C, Tala A, Spinosa MR, Progida C, De Nitto E, Gaballo A, Bruni CB, Bucci C, Alifano P. (literal)
Pagina inizio
  • 1725 (literal)
Pagina fine
  • 1740 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 74 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomembranes and Bioenergetics C.N.R.-Bari Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università di Lecce Dipartimento di Biologia e Patologia Cellulare e Molecolare \"L. Califano\", Università di Napoli \"Federico II\", Istituto di Endocrinologia ed Oncologia 12 Sperimentale \"G. Salvatore\" C.N.R. 80131 Napoli (literal)
Titolo
  • Identification of a Meningococcal L-glutamate ABC Transporter operon essential for growth in low-sodium environments (literal)
Abstract
  • GdhR is a meningococcal transcriptional regulator that was previously shown to positively control the expression of gdhA, encoding the NADP-specific L-glutamate dehydrogenase (NADP-GDH), in response to the growth phase and/or to the carbon source. In this study we used reverse transcriptase-PCR-differential display (to identify additional GdhR-regulated genes. The results indicated that GdhR, in addition to NADP-GDH, controls the expression of a number of genes involved in glucose catabolism by the Entner-Doudoroff pathway and in l-glutamate import by an unknown ABC transport system. The genes encoding the putative periplasmic substrate-binding protein (NMB1963) and the permease (NMB1965) of the ABC transporter were genetically inactivated. Uptake experiments demonstrated an impairment of L-glutamate import in the NMB1965-defective mutant in the absence or in the presence of a low sodium ion concentration. In contrast, at a sodium ion concentration above 60 mM, the uptake defect disappeared, possibly because the activity of a sodium-driven secondary transporter became predominant. Indeed, the NMB1965-defective mutant was unable to grow at a low sodium ion concentration (<20 mM) in a chemically defined medium containing L-glutamate and four other amino acids that supported meningococcal growth, but it grew when the sodium ion concentration was raised to higher values (>60 mM). The same growth phenotype was observed in the NMB1963-defective mutant. Cell invasion and intracellular persistence assays and expression data during cell invasion provided evidence that the l-glutamate ABC transporter, tentatively named GltT, was critical for meningococcal adaptation in the low-sodium intracellular environment. (literal)
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