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dc.contributor.author
Vincent, Paula Andrea
dc.contributor.author
Morero, Roberto Dionisio
dc.date.available
2018-12-07T15:44:40Z
dc.date.issued
2009-03
dc.identifier.citation
Vincent, Paula Andrea; Morero, Roberto Dionisio; The structure and biological aspects of peptide antibiotic microcin J25; Bentham Science Publishers; Current Medicinal Chemistry; 16; 5; 3-2009; 538-549
dc.identifier.issn
0929-8673
dc.identifier.uri
http://hdl.handle.net/11336/66054
dc.description.abstract
Microcin J25 (MccJ25) is a plasmid-encoded peptide of 21 L-amino acids (G1-G-A-G-H5-V-P-E-Y-F10-V-G- I-G-T15-P-I-S-F-Y20-G), excreted to the medium by an Escherichia coli strain. MccJ25 is active on Gram-negative bacteria related to the producer strain, including some pathogenic strains. The four-plasmid genes mcjABCD, are involved in MccJ25 production: mcjA encodes a 58-residue precursor, mcjB and mcjC codify two processing enzymes required for the in vivo synthesis of the mature peptide and mcjD encodes the immunity protein (McjD), a member of the super family of ABC transporters. Immunity is mediated by active efflux of the peptide, keeping its intracellular concentration below a critical level. YojI, a chromosomal protein with ATP-binding-cassette-type exporter homology, is also able to export MccJ25. The E. coli outer membrane protein, TolC, is necessary for MccJ25 secretion mediated by either McjD or YojI. The uptake of MccJ25 is dependent on the outer-membrane receptor FhuA and the four inner-membrane proteins TonB, ExbD, ExbB and SbmA. At least two mechanisms described the action of MccJ25 on the target cells: (1) inhibition of the RNA-polymerase (RNAP) activity by obstructing the secondary channel, and consequently, preventing the access of the substrates to its active sites; and (2) operating on the cell membrane, MccJ25 disrupts the electric potential inhibiting the oxygen consumption in Salmonella enterica. MccJ25 also inhibits oxygen consumption and the respiratory chain enzymes in E. coli throughout the increasing of ROS concentration. Nevertheless the exact mechanism of this phenomenon must be elucidated. The MccJ25 exhibits a prolonged antimicrobial activity in a mouse infection model, suggesting a noteworthy potential for therapeutic uses.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Bentham Science Publishers
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Antibiotics
dc.subject
Enterobacteriaceae
dc.subject
Microcins
dc.subject
Peptide
dc.subject.classification
Otras Ciencias Biológicas
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The structure and biological aspects of peptide antibiotic microcin J25
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-11-13T14:05:55Z
dc.journal.volume
16
dc.journal.number
5
dc.journal.pagination
538-549
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Oak Park
dc.description.fil
Fil: Vincent, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Morero, Roberto Dionisio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.journal.title
Current Medicinal Chemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.2174/092986709787458461
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://benthamscience.com/journals/current-medicinal-chemistry/volume/16/issue/5/page/538/
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