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

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)658-665
Number of pages8
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1818
Issue number3
DOIs
Publication statusPublished - Mar 1 2012

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding'. Together they form a unique fingerprint.

  • Cite this