TY  - JOUR
AU  - Gajić, O
AU  - Buist, G
AU  - Kojić, Milan
AU  - Topisirović, Ljubiša
AU  - Kuipers, OP
AU  - Kok, J
PY  - 2003
UR  - http://intor.torlakinstitut.com/handle/123456789/800
AB  - A natural isolate of Lactococcus lactis was shown to produce two narrow spectrum class II bacteriocins, designated LsbA and LsbB. The cognate genes are located on a 5.6-kb plasmid within a gene cluster specifying LmrB, an ATP-binding cassette-type multidrug resistance transporter protein. LsbA is a hydrophobic peptide that is initially synthesized with an N-terminal extension. The housekeeping surface proteinase HtrA was shown to be responsible for the cleavage of precursor peptide to yield the active bacteriocin. LsbB is a relatively hydrophilic protein synthesized without an N-terminal leader sequence or signal peptide. The secretion of both polypeptides was shown to be mediated by LmrB. An L. lactis strain lacking plasmid-encoded LmrB and the chromosomally encoded LmrA is unable to secrete either of the two bacteriocins. Complementation of the strain with an active LmrB protein resulted in restored export of the two polypeptides across the cytoplasmic membrane. When expressed in an L. lactis strain that is sensitive to LsbA and LsbB, LmrB was shown to confer resistance toward both bacteriocins. It does so, most likely, by removing the two polypeptides from the cytoplasmic membrane. This is the first report in which a multidrug transporter protein is shown to be involved in both secretion and immunity of antimicrobial peptides.
PB  - Amer Soc Biochemistry Molecular Biology Inc, Bethesda
T2  - Journal of Biological Chemistry
T1  - Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins
EP  - 34298
IS  - 36
SP  - 34291
VL  - 278
DO  - 10.1074/jbc.M211100200
ER  - 

@article{
author = "Gajić, O and Buist, G and Kojić, Milan and Topisirović, Ljubiša and Kuipers, OP and Kok, J",
year = "2003",
abstract = "A natural isolate of Lactococcus lactis was shown to produce two narrow spectrum class II bacteriocins, designated LsbA and LsbB. The cognate genes are located on a 5.6-kb plasmid within a gene cluster specifying LmrB, an ATP-binding cassette-type multidrug resistance transporter protein. LsbA is a hydrophobic peptide that is initially synthesized with an N-terminal extension. The housekeeping surface proteinase HtrA was shown to be responsible for the cleavage of precursor peptide to yield the active bacteriocin. LsbB is a relatively hydrophilic protein synthesized without an N-terminal leader sequence or signal peptide. The secretion of both polypeptides was shown to be mediated by LmrB. An L. lactis strain lacking plasmid-encoded LmrB and the chromosomally encoded LmrA is unable to secrete either of the two bacteriocins. Complementation of the strain with an active LmrB protein resulted in restored export of the two polypeptides across the cytoplasmic membrane. When expressed in an L. lactis strain that is sensitive to LsbA and LsbB, LmrB was shown to confer resistance toward both bacteriocins. It does so, most likely, by removing the two polypeptides from the cytoplasmic membrane. This is the first report in which a multidrug transporter protein is shown to be involved in both secretion and immunity of antimicrobial peptides.",
publisher = "Amer Soc Biochemistry Molecular Biology Inc, Bethesda",
journal = "Journal of Biological Chemistry",
title = "Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins",
pages = "34298-34291",
number = "36",
volume = "278",
doi = "10.1074/jbc.M211100200"
}

Gajić, O., Buist, G., Kojić, M., Topisirović, L., Kuipers, O.,& Kok, J.. (2003). Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins. in Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc, Bethesda., 278(36), 34291-34298.
https://doi.org/10.1074/jbc.M211100200

Gajić O, Buist G, Kojić M, Topisirović L, Kuipers O, Kok J. Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins. in Journal of Biological Chemistry. 2003;278(36):34291-34298.
doi:10.1074/jbc.M211100200 .

Gajić, O, Buist, G, Kojić, Milan, Topisirović, Ljubiša, Kuipers, OP, Kok, J, "Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins" in Journal of Biological Chemistry, 278, no. 36 (2003):34291-34298,
https://doi.org/10.1074/jbc.M211100200 . .