R76 in transmembrane domain 3 of the aspartate:alanine transporter AspT is involved in substrate transport

Satomi Suzuki; Kei Nanatani; Keietsu Abe

doi:10.1080/09168451.2015.1123609

R76 in transmembrane domain 3 of the aspartate:alanine transporter AspT is involved in substrate transport

Satomi Suzuki, Kei Nanatani, Keietsu Abe

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

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Abstract

The L-aspartate:L-alanine antiporter of Tetragenococcus halophilus (AspT) possesses an arginine residue (R76) within the GxxxG motif in the central part of transmembrane domain 3 (TM3) - a residue that has been estimated to transport function. In this study, we carried out amino acid substitutions of R76 and used proteoliposome reconstitution for analyzing the transport function of each substitution. Both L-aspartate and L-alanine transport assays showed that R76K has higher activity than the AspT-WT (R76), whereas R76D and R76E have lower activity than the AspT-WT. These results suggest that R76 is involved in AspT substrate transport.

Original language	English
Pages (from-to)	744-747
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	80
Issue number	4
DOIs	https://doi.org/10.1080/09168451.2015.1123609
Publication status	Published - 2016

Keywords

Amino acid transporter
GxxxG
Liposome
Substrate transport
Transport activity

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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10.1080/09168451.2015.1123609

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title = "R76 in transmembrane domain 3 of the aspartate:alanine transporter AspT is involved in substrate transport",

abstract = "The L-aspartate:L-alanine antiporter of Tetragenococcus halophilus (AspT) possesses an arginine residue (R76) within the GxxxG motif in the central part of transmembrane domain 3 (TM3) - a residue that has been estimated to transport function. In this study, we carried out amino acid substitutions of R76 and used proteoliposome reconstitution for analyzing the transport function of each substitution. Both L-aspartate and L-alanine transport assays showed that R76K has higher activity than the AspT-WT (R76), whereas R76D and R76E have lower activity than the AspT-WT. These results suggest that R76 is involved in AspT substrate transport.",

keywords = "Amino acid transporter, GxxxG, Liposome, Substrate transport, Transport activity",

author = "Satomi Suzuki and Kei Nanatani and Keietsu Abe",

note = "Funding Information: This work was supported partly by KAKENHI, a Grant-in-Aid for Challenging Exploratory Research (Japan Society for the Promotion of Science; [grant number 2265108 and 15K14911] to K. A., and Grant-in-Aid for JSPS Fellows [grant number 25•3082] to S. S.). This study was also partly supported by an NISR Research Grant from the Noda Institute for Scientific Research (to K. A.). Publisher Copyright: {\textcopyright} 2016 Japan Society for Bioscience, Biotechnology, and Agrochemistry.",

year = "2016",

doi = "10.1080/09168451.2015.1123609",

language = "English",

volume = "80",

pages = "744--747",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "4",

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TY - JOUR

T1 - R76 in transmembrane domain 3 of the aspartate:alanine transporter AspT is involved in substrate transport

AU - Suzuki, Satomi

AU - Nanatani, Kei

AU - Abe, Keietsu

N1 - Funding Information: This work was supported partly by KAKENHI, a Grant-in-Aid for Challenging Exploratory Research (Japan Society for the Promotion of Science; [grant number 2265108 and 15K14911] to K. A., and Grant-in-Aid for JSPS Fellows [grant number 25•3082] to S. S.). This study was also partly supported by an NISR Research Grant from the Noda Institute for Scientific Research (to K. A.). Publisher Copyright: © 2016 Japan Society for Bioscience, Biotechnology, and Agrochemistry.

PY - 2016

Y1 - 2016

N2 - The L-aspartate:L-alanine antiporter of Tetragenococcus halophilus (AspT) possesses an arginine residue (R76) within the GxxxG motif in the central part of transmembrane domain 3 (TM3) - a residue that has been estimated to transport function. In this study, we carried out amino acid substitutions of R76 and used proteoliposome reconstitution for analyzing the transport function of each substitution. Both L-aspartate and L-alanine transport assays showed that R76K has higher activity than the AspT-WT (R76), whereas R76D and R76E have lower activity than the AspT-WT. These results suggest that R76 is involved in AspT substrate transport.

AB - The L-aspartate:L-alanine antiporter of Tetragenococcus halophilus (AspT) possesses an arginine residue (R76) within the GxxxG motif in the central part of transmembrane domain 3 (TM3) - a residue that has been estimated to transport function. In this study, we carried out amino acid substitutions of R76 and used proteoliposome reconstitution for analyzing the transport function of each substitution. Both L-aspartate and L-alanine transport assays showed that R76K has higher activity than the AspT-WT (R76), whereas R76D and R76E have lower activity than the AspT-WT. These results suggest that R76 is involved in AspT substrate transport.

KW - Amino acid transporter

KW - GxxxG

KW - Liposome

KW - Substrate transport

KW - Transport activity

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U2 - 10.1080/09168451.2015.1123609

DO - 10.1080/09168451.2015.1123609

M3 - Article

C2 - 26849958

AN - SCOPUS:84962409111

SN - 0916-8451

VL - 80

SP - 744

EP - 747

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 4

ER -

R76 in transmembrane domain 3 of the aspartate:alanine transporter AspT is involved in substrate transport

Abstract

Keywords

ASJC Scopus subject areas

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