Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding

Shinya Takazaki, Yoshito Abe, Tomohiro Yamaguchi, Mikako Yagi, Tadashi Ueda, Dongchon Kang, Naotaka Hamasaki

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

In our previous paper, we demonstrated that Arg 901 in the C-terminal tail of human AE1 (band 3, anion exchanger 1) had a functional role in conformational change during anion exchange. To further examine how Arg 901 is involved in conformational change, we expressed various Arg 901 mutants and alanine mutants of the C-terminal tail (from Leu 886 to Val 911) on the plasma membrane of Saccharomyces cerevisiae and evaluated the kinetic parameters of sulfate ion transport. As a result, Vmax decreased as the hydrophobicities of the 901st and peripheral hydrophilic residues increased, indicating that the hydrophobicity of the C-terminal residue is involved in the conformational change. We also found the alkali and protease resistance of the C-terminal region after Arg 901 modification with hydroxyphenylglyoxal (HPG) or phenylglyoxal (PG), a hydrophobic reagent. These results suggested that the increased hydrophobicity of the C-terminal region around Arg 901 leads to inefficient conformational change by the newly produced hydrophobic interaction.

元の言語英語
ページ(範囲)658-665
ページ数8
ジャーナルBiochimica et Biophysica Acta - Biomembranes
1818
発行部数3
DOI
出版物ステータス出版済み - 3 1 2012

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Erythrocyte Anion Exchange Protein 1
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Tail
Substrates
Phenylglyoxal
Alkalies
Cell membranes
Kinetic parameters
Alanine
Yeast
Sulfates
Anions
Ion Transport
Peptide Hydrolases
Ions
Saccharomyces cerevisiae
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

これを引用

Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding. / Takazaki, Shinya; Abe, Yoshito; Yamaguchi, Tomohiro; Yagi, Mikako; Ueda, Tadashi; Kang, Dongchon; Hamasaki, Naotaka.

:: Biochimica et Biophysica Acta - Biomembranes, 巻 1818, 番号 3, 01.03.2012, p. 658-665.

研究成果: ジャーナルへの寄稿記事

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abstract = "In our previous paper, we demonstrated that Arg 901 in the C-terminal tail of human AE1 (band 3, anion exchanger 1) had a functional role in conformational change during anion exchange. To further examine how Arg 901 is involved in conformational change, we expressed various Arg 901 mutants and alanine mutants of the C-terminal tail (from Leu 886 to Val 911) on the plasma membrane of Saccharomyces cerevisiae and evaluated the kinetic parameters of sulfate ion transport. As a result, Vmax decreased as the hydrophobicities of the 901st and peripheral hydrophilic residues increased, indicating that the hydrophobicity of the C-terminal residue is involved in the conformational change. We also found the alkali and protease resistance of the C-terminal region after Arg 901 modification with hydroxyphenylglyoxal (HPG) or phenylglyoxal (PG), a hydrophobic reagent. These results suggested that the increased hydrophobicity of the C-terminal region around Arg 901 leads to inefficient conformational change by the newly produced hydrophobic interaction.",
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T1 - Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding

AU - Takazaki, Shinya

AU - Abe, Yoshito

AU - Yamaguchi, Tomohiro

AU - Yagi, Mikako

AU - Ueda, Tadashi

AU - Kang, Dongchon

AU - Hamasaki, Naotaka

PY - 2012/3/1

Y1 - 2012/3/1

N2 - In our previous paper, we demonstrated that Arg 901 in the C-terminal tail of human AE1 (band 3, anion exchanger 1) had a functional role in conformational change during anion exchange. To further examine how Arg 901 is involved in conformational change, we expressed various Arg 901 mutants and alanine mutants of the C-terminal tail (from Leu 886 to Val 911) on the plasma membrane of Saccharomyces cerevisiae and evaluated the kinetic parameters of sulfate ion transport. As a result, Vmax decreased as the hydrophobicities of the 901st and peripheral hydrophilic residues increased, indicating that the hydrophobicity of the C-terminal residue is involved in the conformational change. We also found the alkali and protease resistance of the C-terminal region after Arg 901 modification with hydroxyphenylglyoxal (HPG) or phenylglyoxal (PG), a hydrophobic reagent. These results suggested that the increased hydrophobicity of the C-terminal region around Arg 901 leads to inefficient conformational change by the newly produced hydrophobic interaction.

AB - In our previous paper, we demonstrated that Arg 901 in the C-terminal tail of human AE1 (band 3, anion exchanger 1) had a functional role in conformational change during anion exchange. To further examine how Arg 901 is involved in conformational change, we expressed various Arg 901 mutants and alanine mutants of the C-terminal tail (from Leu 886 to Val 911) on the plasma membrane of Saccharomyces cerevisiae and evaluated the kinetic parameters of sulfate ion transport. As a result, Vmax decreased as the hydrophobicities of the 901st and peripheral hydrophilic residues increased, indicating that the hydrophobicity of the C-terminal residue is involved in the conformational change. We also found the alkali and protease resistance of the C-terminal region after Arg 901 modification with hydroxyphenylglyoxal (HPG) or phenylglyoxal (PG), a hydrophobic reagent. These results suggested that the increased hydrophobicity of the C-terminal region around Arg 901 leads to inefficient conformational change by the newly produced hydrophobic interaction.

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