PMID- 16237035
OWN - NLM
STAT- MEDLINE
DCOM- 20051129
LR  - 20181113
IS  - 0021-9193 (Print)
IS  - 1098-5530 (Electronic)
IS  - 0021-9193 (Linking)
VI  - 187
IP  - 21
DP  - 2005 Nov
TI  - Characterization of bacterial drug antiporters homologous to mammalian 
      neurotransmitter transporters.
PG  - 7518-25
AB  - Multidrug transporters are ubiquitous proteins, and, based on amino acid sequence 
      similarities, they have been classified into several families. Here we 
      characterize a cluster of archaeal and bacterial proteins from the major 
      facilitator superfamily (MFS). One member of this family, the vesicular monoamine 
      transporter (VMAT) was previously shown to remove both neurotransmitters and 
      toxic compounds from the cytoplasm, thereby conferring resistance to their 
      effects. A BLAST search of the available microbial genomes against the VMAT 
      sequence yielded sequences of novel putative multidrug transporters. The new 
      sequences along with VMAT form a distinct cluster within the dendrogram of the 
      MFS, drug-proton antiporters. A comparison with other proteins in the family 
      suggests the existence of a potential ion pair in the membrane domain. Three of 
      these genes, from Mycobacterium smegmatis, Corynebacterium glutamicum, and 
      Halobacterium salinarum, were cloned and functionally expressed in Escherichia 
      coli. The proteins conferred resistance to fluoroquinolones and chloramphenicol 
      (at concentrations two to four times greater than that of the control). 
      Measurement of antibiotic accumulation in cells revealed proton motive 
      force-dependent transport of those compounds.
FAU - Vardy, Eyal
AU  - Vardy E
AD  - Department of Biological Chemistry, Alexander Silberman Institute of Life 
      Sciences, Hebrew University of Jerusalem, Jerusalem, Israel. 
      Shimon.Schuldiner@huji.ac.il.
FAU - Steiner-Mordoch, Sonia
AU  - Steiner-Mordoch S
FAU - Schuldiner, Shimon
AU  - Schuldiner S
LA  - eng
GR  - P50 GM073210/GM/NIGMS NIH HHS/United States
GR  - P50 GM73210/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Antiporters)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Fluoroquinolones)
RN  - 0 (Recombinant Proteins)
RN  - 66974FR9Q1 (Chloramphenicol)
SB  - IM
MH  - Amino Acid Sequence
MH  - Anti-Bacterial Agents/*pharmacology
MH  - Antiporters/chemistry/*genetics/physiology
MH  - Archaea/*metabolism
MH  - Bacteria/*metabolism
MH  - Bacterial Proteins/chemistry/*genetics/metabolism/physiology
MH  - *Biological Transport
MH  - Chloramphenicol/pharmacology
MH  - Cloning, Molecular
MH  - Corynebacterium glutamicum/genetics
MH  - Drug Resistance, Multiple, Bacterial/*genetics/physiology
MH  - Escherichia coli/drug effects
MH  - Fluoroquinolones/pharmacology
MH  - Genes, Bacterial
MH  - Halobacterium salinarum/genetics
MH  - Molecular Sequence Data
MH  - Mycobacterium smegmatis/genetics
MH  - Phylogeny
MH  - Protein Conformation
MH  - Recombinant Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
PMC - PMC1272986
EDAT- 2005/10/21 09:00
MHDA- 2005/12/13 09:00
PMCR- 2005/11/01
CRDT- 2005/10/21 09:00
PHST- 2005/10/21 09:00 [pubmed]
PHST- 2005/12/13 09:00 [medline]
PHST- 2005/10/21 09:00 [entrez]
PHST- 2005/11/01 00:00 [pmc-release]
AID - 187/21/7518 [pii]
AID - 0765-05 [pii]
AID - 10.1128/JB.187.21.7518-7525.2005 [doi]
PST - ppublish
SO  - J Bacteriol. 2005 Nov;187(21):7518-25. doi: 10.1128/JB.187.21.7518-7525.2005.