Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus

Kei Nanatani; Fumito Ohonishi; Hiroshi Yoneyama; Tasuku Nakajima; Keietsu Abe

doi:10.1016/j.bbrc.2004.12.133

Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus

Kei Nanatani, Fumito Ohonishi, Hiroshi Yoneyama, Tasuku Nakajima, Keietsu Abe

AGR - Bioscience and Biotechnology for Future Bioindustries

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

7 Citations (Scopus)

Abstract

AspT is an electrogenic aspartate:alanine exchange protein that represents the vectorial component of a proton-motive metabolic cycle found in some strains of Tetragenococcus halophilus. AspT is the sole member of a new family, the Aspartate: Alanine Exchanger (AAE) family, in secondary transporters, according to the computational classification proposed by Saier et al. (http://www.biology.ucsd.edu/~msaier/transport/). We analyzed the topology of AspT biochemically, by using fusion methods in combination with alkaline phosphatase or β-lactamase. These results suggested that AspT has a unique topology; 8 TMS, a large cytoplasmic loop (183 amino acids) between TMS5 and TMS6, and N- and C-termini that both face the periplasm. These results demonstrated a unique 2D-structure of AspT as the novel AAE family.

Original language	English
Pages (from-to)	20-26
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	328
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2004.12.133
Publication status	Published - 2005 Mar 4

Keywords

Aspartate:Alanine Antiporter
Electrogenic
Fusion methods
Membrane topology
Proton-motive force

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus",

abstract = "AspT is an electrogenic aspartate:alanine exchange protein that represents the vectorial component of a proton-motive metabolic cycle found in some strains of Tetragenococcus halophilus. AspT is the sole member of a new family, the Aspartate: Alanine Exchanger (AAE) family, in secondary transporters, according to the computational classification proposed by Saier et al. (http://www.biology.ucsd.edu/~msaier/transport/). We analyzed the topology of AspT biochemically, by using fusion methods in combination with alkaline phosphatase or β-lactamase. These results suggested that AspT has a unique topology; 8 TMS, a large cytoplasmic loop (183 amino acids) between TMS5 and TMS6, and N- and C-termini that both face the periplasm. These results demonstrated a unique 2D-structure of AspT as the novel AAE family.",

keywords = "Aspartate:Alanine Antiporter, Electrogenic, Fusion methods, Membrane topology, Proton-motive force",

author = "Kei Nanatani and Fumito Ohonishi and Hiroshi Yoneyama and Tasuku Nakajima and Keietsu Abe",

year = "2005",

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doi = "10.1016/j.bbrc.2004.12.133",

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T1 - Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus

AU - Nanatani, Kei

AU - Ohonishi, Fumito

AU - Yoneyama, Hiroshi

AU - Nakajima, Tasuku

AU - Abe, Keietsu

PY - 2005/3/4

Y1 - 2005/3/4

N2 - AspT is an electrogenic aspartate:alanine exchange protein that represents the vectorial component of a proton-motive metabolic cycle found in some strains of Tetragenococcus halophilus. AspT is the sole member of a new family, the Aspartate: Alanine Exchanger (AAE) family, in secondary transporters, according to the computational classification proposed by Saier et al. (http://www.biology.ucsd.edu/~msaier/transport/). We analyzed the topology of AspT biochemically, by using fusion methods in combination with alkaline phosphatase or β-lactamase. These results suggested that AspT has a unique topology; 8 TMS, a large cytoplasmic loop (183 amino acids) between TMS5 and TMS6, and N- and C-termini that both face the periplasm. These results demonstrated a unique 2D-structure of AspT as the novel AAE family.

AB - AspT is an electrogenic aspartate:alanine exchange protein that represents the vectorial component of a proton-motive metabolic cycle found in some strains of Tetragenococcus halophilus. AspT is the sole member of a new family, the Aspartate: Alanine Exchanger (AAE) family, in secondary transporters, according to the computational classification proposed by Saier et al. (http://www.biology.ucsd.edu/~msaier/transport/). We analyzed the topology of AspT biochemically, by using fusion methods in combination with alkaline phosphatase or β-lactamase. These results suggested that AspT has a unique topology; 8 TMS, a large cytoplasmic loop (183 amino acids) between TMS5 and TMS6, and N- and C-termini that both face the periplasm. These results demonstrated a unique 2D-structure of AspT as the novel AAE family.

KW - Aspartate:Alanine Antiporter

KW - Electrogenic

KW - Fusion methods

KW - Membrane topology

KW - Proton-motive force

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