Membrane topology of the GltS Na+/glutamate permease of Escherichia coli

Attila Szvetnik; József Gál; Miklós Kálmán

doi:10.1111/j.1574-6968.2007.00863.x

Membrane topology of the GltS Na⁺/glutamate permease of Escherichia coli

Attila Szvetnik, József Gál, Miklós Kálmán

Neuroscience

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The GltS Na⁺/glutamate permease of Escherichia coli is the most extensively studied member of the ESS family of bacterial glutamate : Na ⁺ symporters. This paper presents the membrane topology analysis of the GltS with translational alkaline phosphatase and β-galactosidase gene fusions generated by TnphoA, nested deletions and targeted fusions. The topology model suggested by the translational fusion technique is compared with the MemGen model and discussed in detail.

Original language	English
Pages (from-to)	71-79
Number of pages	9
Journal	FEMS Microbiology Letters
Volume	275
Issue number	1
DOIs	https://doi.org/10.1111/j.1574-6968.2007.00863.x
State	Published - Oct 2007

Keywords

GltS
Glutamate
LacZ
PhoA
Pore-loop
Topology

ASJC Scopus subject areas

Microbiology
Molecular Biology
Genetics

Access to Document

10.1111/j.1574-6968.2007.00863.x

Cite this

@article{6e1eef7d02514dc1894afd07613317a1,

title = "Membrane topology of the GltS Na+/glutamate permease of Escherichia coli",

abstract = "The GltS Na+/glutamate permease of Escherichia coli is the most extensively studied member of the ESS family of bacterial glutamate : Na + symporters. This paper presents the membrane topology analysis of the GltS with translational alkaline phosphatase and β-galactosidase gene fusions generated by TnphoA, nested deletions and targeted fusions. The topology model suggested by the translational fusion technique is compared with the MemGen model and discussed in detail.",

keywords = "GltS, Glutamate, LacZ, PhoA, Pore-loop, Topology",

author = "Attila Szvetnik and J{\'o}zsef G{\'a}l and Mikl{\'o}s K{\'a}lm{\'a}n",

year = "2007",

month = oct,

doi = "10.1111/j.1574-6968.2007.00863.x",

language = "English",

volume = "275",

pages = "71--79",

number = "1",

}

TY - JOUR

T1 - Membrane topology of the GltS Na+/glutamate permease of Escherichia coli

AU - Szvetnik, Attila

AU - Gál, József

AU - Kálmán, Miklós

PY - 2007/10

Y1 - 2007/10

N2 - The GltS Na+/glutamate permease of Escherichia coli is the most extensively studied member of the ESS family of bacterial glutamate : Na + symporters. This paper presents the membrane topology analysis of the GltS with translational alkaline phosphatase and β-galactosidase gene fusions generated by TnphoA, nested deletions and targeted fusions. The topology model suggested by the translational fusion technique is compared with the MemGen model and discussed in detail.

AB - The GltS Na+/glutamate permease of Escherichia coli is the most extensively studied member of the ESS family of bacterial glutamate : Na + symporters. This paper presents the membrane topology analysis of the GltS with translational alkaline phosphatase and β-galactosidase gene fusions generated by TnphoA, nested deletions and targeted fusions. The topology model suggested by the translational fusion technique is compared with the MemGen model and discussed in detail.

KW - GltS

KW - Glutamate

KW - LacZ

KW - PhoA

KW - Pore-loop

KW - Topology

UR - http://www.scopus.com/inward/record.url?scp=34548585249&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34548585249&partnerID=8YFLogxK

U2 - 10.1111/j.1574-6968.2007.00863.x

DO - 10.1111/j.1574-6968.2007.00863.x

M3 - Article

C2 - 17662058

AN - SCOPUS:34548585249

SN - 0378-1097

VL - 275

SP - 71

EP - 79

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -