Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt

Dale P Woolridge, Nora Vazquez-Laslop, Penelope N. Markham, Mathieu S. Chevalier, Eugene W. Gerner, Alexander A. Neyfakh

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

Multidrug transporters pump structurally dissimilar toxic molecules out of cells. It is not known, however, if detoxification is the primary physiological function of these transporters. The chromosomal organization of the gene encoding the Bacillus subtilis multidrug transporter Blt suggests a specific function for this protein; it forms a single operon with another gene, bltD, whose protein product is identified here as a spermine/spermidine acetyltransferase, an enzyme catalyzing a key step in spermidine degradation. Overexpression of the Blt transporter in B. subtilis leads not only to the multidrug-resistance phenotype but also to the efflux of large amounts of spermidine into the medium; this efflux is suppressed by an inhibitor of Blt, reserpine. Taken together, these results strongly suggest that the natural function of the Blt transporter is the efflux of spermidine, whereas multiple drugs may be recognized by Blt merely opportunistically.

Original languageEnglish (US)
Pages (from-to)8864-8866
Number of pages3
JournalJournal of Biological Chemistry
Volume272
Issue number14
DOIs
StatePublished - Apr 4 1997

Fingerprint

Spermidine
Polyamines
Bacilli
Bacillus subtilis
Detoxification
Gene encoding
Spermine
Poisons
Reserpine
Multiple Drug Resistance
Operon
Genes
Proteins
Pumps
Phenotype
Degradation
Molecules
Enzymes
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Biochemistry

Cite this

Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt. / Woolridge, Dale P; Vazquez-Laslop, Nora; Markham, Penelope N.; Chevalier, Mathieu S.; Gerner, Eugene W.; Neyfakh, Alexander A.

In: Journal of Biological Chemistry, Vol. 272, No. 14, 04.04.1997, p. 8864-8866.

Research output: Contribution to journalArticle

Woolridge, Dale P ; Vazquez-Laslop, Nora ; Markham, Penelope N. ; Chevalier, Mathieu S. ; Gerner, Eugene W. ; Neyfakh, Alexander A. / Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt. In: Journal of Biological Chemistry. 1997 ; Vol. 272, No. 14. pp. 8864-8866.
@article{f4e80a474e264efd9a03194070ee57e1,
title = "Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt",
abstract = "Multidrug transporters pump structurally dissimilar toxic molecules out of cells. It is not known, however, if detoxification is the primary physiological function of these transporters. The chromosomal organization of the gene encoding the Bacillus subtilis multidrug transporter Blt suggests a specific function for this protein; it forms a single operon with another gene, bltD, whose protein product is identified here as a spermine/spermidine acetyltransferase, an enzyme catalyzing a key step in spermidine degradation. Overexpression of the Blt transporter in B. subtilis leads not only to the multidrug-resistance phenotype but also to the efflux of large amounts of spermidine into the medium; this efflux is suppressed by an inhibitor of Blt, reserpine. Taken together, these results strongly suggest that the natural function of the Blt transporter is the efflux of spermidine, whereas multiple drugs may be recognized by Blt merely opportunistically.",
author = "Woolridge, {Dale P} and Nora Vazquez-Laslop and Markham, {Penelope N.} and Chevalier, {Mathieu S.} and Gerner, {Eugene W.} and Neyfakh, {Alexander A.}",
year = "1997",
month = "4",
day = "4",
doi = "10.1074/jbc.272.14.8864",
language = "English (US)",
volume = "272",
pages = "8864--8866",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

TY - JOUR

T1 - Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt

AU - Woolridge, Dale P

AU - Vazquez-Laslop, Nora

AU - Markham, Penelope N.

AU - Chevalier, Mathieu S.

AU - Gerner, Eugene W.

AU - Neyfakh, Alexander A.

PY - 1997/4/4

Y1 - 1997/4/4

N2 - Multidrug transporters pump structurally dissimilar toxic molecules out of cells. It is not known, however, if detoxification is the primary physiological function of these transporters. The chromosomal organization of the gene encoding the Bacillus subtilis multidrug transporter Blt suggests a specific function for this protein; it forms a single operon with another gene, bltD, whose protein product is identified here as a spermine/spermidine acetyltransferase, an enzyme catalyzing a key step in spermidine degradation. Overexpression of the Blt transporter in B. subtilis leads not only to the multidrug-resistance phenotype but also to the efflux of large amounts of spermidine into the medium; this efflux is suppressed by an inhibitor of Blt, reserpine. Taken together, these results strongly suggest that the natural function of the Blt transporter is the efflux of spermidine, whereas multiple drugs may be recognized by Blt merely opportunistically.

AB - Multidrug transporters pump structurally dissimilar toxic molecules out of cells. It is not known, however, if detoxification is the primary physiological function of these transporters. The chromosomal organization of the gene encoding the Bacillus subtilis multidrug transporter Blt suggests a specific function for this protein; it forms a single operon with another gene, bltD, whose protein product is identified here as a spermine/spermidine acetyltransferase, an enzyme catalyzing a key step in spermidine degradation. Overexpression of the Blt transporter in B. subtilis leads not only to the multidrug-resistance phenotype but also to the efflux of large amounts of spermidine into the medium; this efflux is suppressed by an inhibitor of Blt, reserpine. Taken together, these results strongly suggest that the natural function of the Blt transporter is the efflux of spermidine, whereas multiple drugs may be recognized by Blt merely opportunistically.

UR - http://www.scopus.com/inward/record.url?scp=0030910587&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030910587&partnerID=8YFLogxK

U2 - 10.1074/jbc.272.14.8864

DO - 10.1074/jbc.272.14.8864

M3 - Article

C2 - 9083003

AN - SCOPUS:0030910587

VL - 272

SP - 8864

EP - 8866

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -