NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli

Yuji Morita, Kazuyo Kodama, Sumiko Shiota, Tomoyuki Mine, Atsuko Kataoka, Tohru Mizushima, Tomofusa Tsuchiya

Research output: Contribution to journalArticle

253 Citations (Scopus)

Abstract

We found that cells of Vibrio parahaemolyticus possess an energy- dependent efflux system for norfloxacin. We cloned a gene for a putative norfloxacin efflux protein from the chromosomal DNA of V. parahaemolyticus by using an Escherichia coli mutant lacking the major multidrug efllux system AcrAB as the host and sequenced the gene (norM). Cells of E. coli transformed with a plasmid carrying the norm gene showed elevated energy-dependent efflux of norfloxacin. The transformants showed elevated resistance not only to norfloxacin and ciprofloxacin but also to the structurally unrelated compounds ethidium, kanamycin, and streptomycin. These results suggest that this is a multidrug efflux system. The hydropathy pattern of the deduced amino acid sequence of Norm suggested the presence of 12 transmembrane domains. The deduced primary structure of Norm showed 57% identity and 88% similarity with that of a hypothetical E. coli membrane protein, YdhE. No reported drug efflux protein in the sequence databases showed significant sequence similarity with NorM. Thus, Norm seems to be a novel type of multidrug efflux protein. We cloned the ydhE gene from E. coli. Cells of E. coli transformed with the cloned ydhE gene showed elevated resistance to norfloxacin, ciprofloxacin, acriflavine, and tetraphenylphosphonium ion, but not to ethidium, when MICs were measured. Thus, it seems that Norm and YdhE differ somehow in substrate specificity.

Original languageEnglish
Pages (from-to)1778-1782
Number of pages5
JournalAntimicrobial Agents and Chemotherapy
Volume42
Issue number7
Publication statusPublished - 1998 Jul
Externally publishedYes

Fingerprint

Vibrio parahaemolyticus
Norfloxacin
Escherichia coli
Ethidium
Genes
Ciprofloxacin
Proteins
Acriflavine
Protein Databases
Kanamycin
Escherichia coli Proteins
Streptomycin
Substrate Specificity
Amino Acid Sequence
Membrane Proteins
Plasmids
Ions
DNA
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Pharmacology (medical)

Cite this

Morita, Y., Kodama, K., Shiota, S., Mine, T., Kataoka, A., Mizushima, T., & Tsuchiya, T. (1998). NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli. Antimicrobial Agents and Chemotherapy, 42(7), 1778-1782.

NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli. / Morita, Yuji; Kodama, Kazuyo; Shiota, Sumiko; Mine, Tomoyuki; Kataoka, Atsuko; Mizushima, Tohru; Tsuchiya, Tomofusa.

In: Antimicrobial Agents and Chemotherapy, Vol. 42, No. 7, 07.1998, p. 1778-1782.

Research output: Contribution to journalArticle

Morita, Y, Kodama, K, Shiota, S, Mine, T, Kataoka, A, Mizushima, T & Tsuchiya, T 1998, 'NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli', Antimicrobial Agents and Chemotherapy, vol. 42, no. 7, pp. 1778-1782.
Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T et al. NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli. Antimicrobial Agents and Chemotherapy. 1998 Jul;42(7):1778-1782.
Morita, Yuji ; Kodama, Kazuyo ; Shiota, Sumiko ; Mine, Tomoyuki ; Kataoka, Atsuko ; Mizushima, Tohru ; Tsuchiya, Tomofusa. / NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli. In: Antimicrobial Agents and Chemotherapy. 1998 ; Vol. 42, No. 7. pp. 1778-1782.
@article{a3609ce1f5de4920a29e525d02890b55,
title = "NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli",
abstract = "We found that cells of Vibrio parahaemolyticus possess an energy- dependent efflux system for norfloxacin. We cloned a gene for a putative norfloxacin efflux protein from the chromosomal DNA of V. parahaemolyticus by using an Escherichia coli mutant lacking the major multidrug efllux system AcrAB as the host and sequenced the gene (norM). Cells of E. coli transformed with a plasmid carrying the norm gene showed elevated energy-dependent efflux of norfloxacin. The transformants showed elevated resistance not only to norfloxacin and ciprofloxacin but also to the structurally unrelated compounds ethidium, kanamycin, and streptomycin. These results suggest that this is a multidrug efflux system. The hydropathy pattern of the deduced amino acid sequence of Norm suggested the presence of 12 transmembrane domains. The deduced primary structure of Norm showed 57{\%} identity and 88{\%} similarity with that of a hypothetical E. coli membrane protein, YdhE. No reported drug efflux protein in the sequence databases showed significant sequence similarity with NorM. Thus, Norm seems to be a novel type of multidrug efflux protein. We cloned the ydhE gene from E. coli. Cells of E. coli transformed with the cloned ydhE gene showed elevated resistance to norfloxacin, ciprofloxacin, acriflavine, and tetraphenylphosphonium ion, but not to ethidium, when MICs were measured. Thus, it seems that Norm and YdhE differ somehow in substrate specificity.",
author = "Yuji Morita and Kazuyo Kodama and Sumiko Shiota and Tomoyuki Mine and Atsuko Kataoka and Tohru Mizushima and Tomofusa Tsuchiya",
year = "1998",
month = "7",
language = "English",
volume = "42",
pages = "1778--1782",
journal = "Antimicrobial Agents and Chemotherapy",
issn = "0066-4804",
publisher = "American Society for Microbiology",
number = "7",

}

TY - JOUR

T1 - NorM, putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli

AU - Morita, Yuji

AU - Kodama, Kazuyo

AU - Shiota, Sumiko

AU - Mine, Tomoyuki

AU - Kataoka, Atsuko

AU - Mizushima, Tohru

AU - Tsuchiya, Tomofusa

PY - 1998/7

Y1 - 1998/7

N2 - We found that cells of Vibrio parahaemolyticus possess an energy- dependent efflux system for norfloxacin. We cloned a gene for a putative norfloxacin efflux protein from the chromosomal DNA of V. parahaemolyticus by using an Escherichia coli mutant lacking the major multidrug efllux system AcrAB as the host and sequenced the gene (norM). Cells of E. coli transformed with a plasmid carrying the norm gene showed elevated energy-dependent efflux of norfloxacin. The transformants showed elevated resistance not only to norfloxacin and ciprofloxacin but also to the structurally unrelated compounds ethidium, kanamycin, and streptomycin. These results suggest that this is a multidrug efflux system. The hydropathy pattern of the deduced amino acid sequence of Norm suggested the presence of 12 transmembrane domains. The deduced primary structure of Norm showed 57% identity and 88% similarity with that of a hypothetical E. coli membrane protein, YdhE. No reported drug efflux protein in the sequence databases showed significant sequence similarity with NorM. Thus, Norm seems to be a novel type of multidrug efflux protein. We cloned the ydhE gene from E. coli. Cells of E. coli transformed with the cloned ydhE gene showed elevated resistance to norfloxacin, ciprofloxacin, acriflavine, and tetraphenylphosphonium ion, but not to ethidium, when MICs were measured. Thus, it seems that Norm and YdhE differ somehow in substrate specificity.

AB - We found that cells of Vibrio parahaemolyticus possess an energy- dependent efflux system for norfloxacin. We cloned a gene for a putative norfloxacin efflux protein from the chromosomal DNA of V. parahaemolyticus by using an Escherichia coli mutant lacking the major multidrug efllux system AcrAB as the host and sequenced the gene (norM). Cells of E. coli transformed with a plasmid carrying the norm gene showed elevated energy-dependent efflux of norfloxacin. The transformants showed elevated resistance not only to norfloxacin and ciprofloxacin but also to the structurally unrelated compounds ethidium, kanamycin, and streptomycin. These results suggest that this is a multidrug efflux system. The hydropathy pattern of the deduced amino acid sequence of Norm suggested the presence of 12 transmembrane domains. The deduced primary structure of Norm showed 57% identity and 88% similarity with that of a hypothetical E. coli membrane protein, YdhE. No reported drug efflux protein in the sequence databases showed significant sequence similarity with NorM. Thus, Norm seems to be a novel type of multidrug efflux protein. We cloned the ydhE gene from E. coli. Cells of E. coli transformed with the cloned ydhE gene showed elevated resistance to norfloxacin, ciprofloxacin, acriflavine, and tetraphenylphosphonium ion, but not to ethidium, when MICs were measured. Thus, it seems that Norm and YdhE differ somehow in substrate specificity.

UR - http://www.scopus.com/inward/record.url?scp=0031836031&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031836031&partnerID=8YFLogxK

M3 - Article

VL - 42

SP - 1778

EP - 1782

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

SN - 0066-4804

IS - 7

ER -