Role of the amino terminal region of the ε{lunate} subunit of Escherichia coli H+-ATPase (FoF1)

Masayoshi Jounouchi, Michiyasu Takeyama, Takato Noumi, Yoshinori Moriyama, Masatomo Maeda, Masamitsu Futai

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Escherichia coli strain KF148(SD-) defective in translation of the uncC gene for the ε{lunate} subunit of H+-ATPase could not support growth by oxidative phosphorylation due to lack of F1 binding to Fo (M. Kuki, T. Noumi, M. Maeda, A. Amemura, and M. Futai, 1988, J. Biol. Chem. 263, 17,437-17,442). Mutant uncC genes for ε{lunate} subunits lacking different lengths from the amino terminus were constructed and introduced into strain KF148(SD-). F1 with an ε{lunate} subunit lacking the 15 amino-terminal residues could bind to Fo in a functionally competent manner, indicating that these amino acid residues are not absolutely necessary for formation of a functional enzyme. However, mutant F1 in which the ε{lunate} subunit lacked 16 amino-terminal residues showed defective coupling between ATP hydrolysis (synthesis) and H+-translocation, although the mutant F1 showed partial binding to Fo. These findings suggest that the ε{lunate} subunit is essential for binding of F1 to Fo and for normal H+-translocation. Previously, Kuki et al. (cited above) reported that 60 residues were not necessary for a functional enzyme. However, the mutant with an ε{lunate} subunit lacking 15 residues from the amino terminus and 4 residues from the carboxyl terminus was defective in oxidative phosphorylation, suggesting that both terminal regions affect the conformation of the region essential for a functional enzyme.

Original languageEnglish
Pages (from-to)87-94
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume292
Issue number1
DOIs
Publication statusPublished - 1992
Externally publishedYes

Fingerprint

Proton-Translocating ATPases
Escherichia coli
Oxidative Phosphorylation
Enzymes
Genes
Conformations
Hydrolysis
Adenosine Triphosphate
Amino Acids
Growth

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Role of the amino terminal region of the ε{lunate} subunit of Escherichia coli H+-ATPase (FoF1). / Jounouchi, Masayoshi; Takeyama, Michiyasu; Noumi, Takato; Moriyama, Yoshinori; Maeda, Masatomo; Futai, Masamitsu.

In: Archives of Biochemistry and Biophysics, Vol. 292, No. 1, 1992, p. 87-94.

Research output: Contribution to journalArticle

Jounouchi, Masayoshi ; Takeyama, Michiyasu ; Noumi, Takato ; Moriyama, Yoshinori ; Maeda, Masatomo ; Futai, Masamitsu. / Role of the amino terminal region of the ε{lunate} subunit of Escherichia coli H+-ATPase (FoF1). In: Archives of Biochemistry and Biophysics. 1992 ; Vol. 292, No. 1. pp. 87-94.
@article{0f05fc63bd6c46d1b5197be261d0d0b6,
title = "Role of the amino terminal region of the ε{lunate} subunit of Escherichia coli H+-ATPase (FoF1)",
abstract = "Escherichia coli strain KF148(SD-) defective in translation of the uncC gene for the ε{lunate} subunit of H+-ATPase could not support growth by oxidative phosphorylation due to lack of F1 binding to Fo (M. Kuki, T. Noumi, M. Maeda, A. Amemura, and M. Futai, 1988, J. Biol. Chem. 263, 17,437-17,442). Mutant uncC genes for ε{lunate} subunits lacking different lengths from the amino terminus were constructed and introduced into strain KF148(SD-). F1 with an ε{lunate} subunit lacking the 15 amino-terminal residues could bind to Fo in a functionally competent manner, indicating that these amino acid residues are not absolutely necessary for formation of a functional enzyme. However, mutant F1 in which the ε{lunate} subunit lacked 16 amino-terminal residues showed defective coupling between ATP hydrolysis (synthesis) and H+-translocation, although the mutant F1 showed partial binding to Fo. These findings suggest that the ε{lunate} subunit is essential for binding of F1 to Fo and for normal H+-translocation. Previously, Kuki et al. (cited above) reported that 60 residues were not necessary for a functional enzyme. However, the mutant with an ε{lunate} subunit lacking 15 residues from the amino terminus and 4 residues from the carboxyl terminus was defective in oxidative phosphorylation, suggesting that both terminal regions affect the conformation of the region essential for a functional enzyme.",
author = "Masayoshi Jounouchi and Michiyasu Takeyama and Takato Noumi and Yoshinori Moriyama and Masatomo Maeda and Masamitsu Futai",
year = "1992",
doi = "10.1016/0003-9861(92)90054-Z",
language = "English",
volume = "292",
pages = "87--94",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Role of the amino terminal region of the ε{lunate} subunit of Escherichia coli H+-ATPase (FoF1)

AU - Jounouchi, Masayoshi

AU - Takeyama, Michiyasu

AU - Noumi, Takato

AU - Moriyama, Yoshinori

AU - Maeda, Masatomo

AU - Futai, Masamitsu

PY - 1992

Y1 - 1992

N2 - Escherichia coli strain KF148(SD-) defective in translation of the uncC gene for the ε{lunate} subunit of H+-ATPase could not support growth by oxidative phosphorylation due to lack of F1 binding to Fo (M. Kuki, T. Noumi, M. Maeda, A. Amemura, and M. Futai, 1988, J. Biol. Chem. 263, 17,437-17,442). Mutant uncC genes for ε{lunate} subunits lacking different lengths from the amino terminus were constructed and introduced into strain KF148(SD-). F1 with an ε{lunate} subunit lacking the 15 amino-terminal residues could bind to Fo in a functionally competent manner, indicating that these amino acid residues are not absolutely necessary for formation of a functional enzyme. However, mutant F1 in which the ε{lunate} subunit lacked 16 amino-terminal residues showed defective coupling between ATP hydrolysis (synthesis) and H+-translocation, although the mutant F1 showed partial binding to Fo. These findings suggest that the ε{lunate} subunit is essential for binding of F1 to Fo and for normal H+-translocation. Previously, Kuki et al. (cited above) reported that 60 residues were not necessary for a functional enzyme. However, the mutant with an ε{lunate} subunit lacking 15 residues from the amino terminus and 4 residues from the carboxyl terminus was defective in oxidative phosphorylation, suggesting that both terminal regions affect the conformation of the region essential for a functional enzyme.

AB - Escherichia coli strain KF148(SD-) defective in translation of the uncC gene for the ε{lunate} subunit of H+-ATPase could not support growth by oxidative phosphorylation due to lack of F1 binding to Fo (M. Kuki, T. Noumi, M. Maeda, A. Amemura, and M. Futai, 1988, J. Biol. Chem. 263, 17,437-17,442). Mutant uncC genes for ε{lunate} subunits lacking different lengths from the amino terminus were constructed and introduced into strain KF148(SD-). F1 with an ε{lunate} subunit lacking the 15 amino-terminal residues could bind to Fo in a functionally competent manner, indicating that these amino acid residues are not absolutely necessary for formation of a functional enzyme. However, mutant F1 in which the ε{lunate} subunit lacked 16 amino-terminal residues showed defective coupling between ATP hydrolysis (synthesis) and H+-translocation, although the mutant F1 showed partial binding to Fo. These findings suggest that the ε{lunate} subunit is essential for binding of F1 to Fo and for normal H+-translocation. Previously, Kuki et al. (cited above) reported that 60 residues were not necessary for a functional enzyme. However, the mutant with an ε{lunate} subunit lacking 15 residues from the amino terminus and 4 residues from the carboxyl terminus was defective in oxidative phosphorylation, suggesting that both terminal regions affect the conformation of the region essential for a functional enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0026502132&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026502132&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(92)90054-Z

DO - 10.1016/0003-9861(92)90054-Z

M3 - Article

VL - 292

SP - 87

EP - 94

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -