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The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine

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The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine

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dc.contributor.author Bidart, Gonzalo N.
dc.contributor.author Rodríguez Díaz, Jesús
dc.contributor.author Pérez-Martínez, Gaspar
dc.contributor.author Yebra Yebra, María Jesús
dc.date.accessioned 2018-11-05T14:39:27Z
dc.date.available 2018-11-05T14:39:27Z
dc.date.issued 2018
dc.identifier.citation Bidart, Gonzalo N. Rodríguez Díaz, Jesús Pérez-Martínez, Gaspar Yebra Yebra, María Jesús 2018 The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine Scientific Reports 8 7152 1 12
dc.identifier.uri http://hdl.handle.net/10550/67854
dc.description.abstract The lactose operon (lacTEGF) from Lactobacillus casei strain BL23 has been previously studied. The lacT gene codes for a transcriptional antiterminator, lacE and lacF for the lactose-specific phosphoenolpyruvate: phosphotransferase system (PTSLac) EIICB and EIIA domains, respectively, and lacG for the phospho-β-galactosidase. In this work, we have shown that L. casei is able to metabolize N-acetyllactosamine (LacNAc), a disaccharide present at human milk and intestinal mucosa. The mutant strains BL153 (lacE) and BL155 (lacF) were defective in LacNAc utilization, indicating that the EIICB and EIIA of the PTSLac are involved in the uptake of LacNAc in addition to lactose. Inactivation of lacG abolishes the growth of L. casei in both disaccharides and analysis of LacG activity showed a high selectivity toward phosphorylated compounds, suggesting that LacG is necessary for the hydrolysis of the intracellular phosphorylated lactose and LacNAc. L. casei (lacAB) strain deficient in galactose-6P isomerase showed a growth rate in lactose (0.0293 ± 0.0014 h-1) and in LacNAc (0.0307 ± 0.0009 h-1) significantly lower than the wild-type (0.1010 ± 0.0006 h-1 and 0.0522 ± 0.0005 h-1, respectively), indicating that their galactose moiety is catabolized through the tagatose-6P pathway. Transcriptional analysis showed induction levels of the lac genes ranged from 130 to 320-fold in LacNAc and from 100 to 200-fold in lactose, compared to cells growing in glucose.
dc.language.iso eng
dc.relation.ispartof Scientific Reports, 2018, vol. 8, num. 7152, p. 1-12
dc.subject Lactobacils
dc.subject Bacteris
dc.title The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine
dc.type journal article es_ES
dc.date.updated 2018-11-05T14:39:27Z
dc.identifier.doi 10.1038/s41598-018-25660-w
dc.identifier.idgrec 128075
dc.rights.accessRights open access es_ES

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