The SMR family: A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs

Ian T. Paulsen; Ronald A. Skurray; Roland Tam; Milton H. Saier; Raymond J. Turner; Joel H. Weiner; Edward B. Goldberg; Leonas L. Grinius

doi:10.1111/j.1365-2958.1996.tb02462.x

The SMR family

A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs

Ian T. Paulsen, Ronald A. Skurray, Roland Tam, Milton H. Saier, Raymond J. Turner, Joel H. Weiner, Edward B. Goldberg, Leonas L. Grinius^*

^*Corresponding author for this work

Research output: Contribution to journal › Review article

215 Citations (Scopus)

Abstract

The sequenced members of a novel family of small, hydrophobic, bacterial multidrug-resistance efflux proteins, which we have designated the small multidrug resistance (SMR) protein family, are identified and analysed. Two distinct clusters of proteins were identified within this family: (i) small multidrug efflux systems; and (ii) Sug proteins, potentially involved in the suppression of groEL mutations. Hydropathy and residue distribution analyses of this family suggest a structural model in which the polypeptide chain spans the membrane four times as mildly amphipathic α-helices. The roles of specific residues, a possible mechanistic model of drug efflux, and the primary physiological role(s) of the SMR proteins are discussed.

Original language	English
Pages (from-to)	1167-1175
Number of pages	9
Journal	Molecular Microbiology
Volume	19
Issue number	6
DOIs	https://doi.org/10.1111/j.1365-2958.1996.tb02462.x
Publication status	Published - 1996
Externally published	Yes

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@article{3c718eaa49be4a13aef66f0020572598,

title = "The SMR family: A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs",

abstract = "The sequenced members of a novel family of small, hydrophobic, bacterial multidrug-resistance efflux proteins, which we have designated the small multidrug resistance (SMR) protein family, are identified and analysed. Two distinct clusters of proteins were identified within this family: (i) small multidrug efflux systems; and (ii) Sug proteins, potentially involved in the suppression of groEL mutations. Hydropathy and residue distribution analyses of this family suggest a structural model in which the polypeptide chain spans the membrane four times as mildly amphipathic α-helices. The roles of specific residues, a possible mechanistic model of drug efflux, and the primary physiological role(s) of the SMR proteins are discussed.",

author = "Paulsen, {Ian T.} and Skurray, {Ronald A.} and Roland Tam and Saier, {Milton H.} and Turner, {Raymond J.} and Weiner, {Joel H.} and Goldberg, {Edward B.} and Grinius, {Leonas L.}",

year = "1996",

doi = "10.1111/j.1365-2958.1996.tb02462.x",

language = "English",

volume = "19",

pages = "1167--1175",

journal = "Molecular Microbiology",

issn = "0950-382X",

publisher = "Wiley-Blackwell, Wiley",

number = "6",

}

The SMR family : A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs. / Paulsen, Ian T.; Skurray, Ronald A.; Tam, Roland; Saier, Milton H.; Turner, Raymond J.; Weiner, Joel H.; Goldberg, Edward B.; Grinius, Leonas L.

In: Molecular Microbiology, Vol. 19, No. 6, 1996, p. 1167-1175.

Research output: Contribution to journal › Review article

TY - JOUR

T1 - The SMR family

T2 - A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs

AU - Paulsen, Ian T.

AU - Skurray, Ronald A.

AU - Tam, Roland

AU - Saier, Milton H.

AU - Turner, Raymond J.

AU - Weiner, Joel H.

AU - Goldberg, Edward B.

AU - Grinius, Leonas L.

PY - 1996

Y1 - 1996

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AB - The sequenced members of a novel family of small, hydrophobic, bacterial multidrug-resistance efflux proteins, which we have designated the small multidrug resistance (SMR) protein family, are identified and analysed. Two distinct clusters of proteins were identified within this family: (i) small multidrug efflux systems; and (ii) Sug proteins, potentially involved in the suppression of groEL mutations. Hydropathy and residue distribution analyses of this family suggest a structural model in which the polypeptide chain spans the membrane four times as mildly amphipathic α-helices. The roles of specific residues, a possible mechanistic model of drug efflux, and the primary physiological role(s) of the SMR proteins are discussed.

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U2 - 10.1111/j.1365-2958.1996.tb02462.x

DO - 10.1111/j.1365-2958.1996.tb02462.x

M3 - Review article

VL - 19

SP - 1167

EP - 1175

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 6

ER -