Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H+-ATPase from mouse cerebellum

Hironori Hanada, Masahisa Hasebe, Yoshinori Moriyama, Masatomo Maeda, Masamitsu Futai

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

cDNa for the 16 kDa subunit of vacuolar H+-ATPase was cloned from mouse cerebellum and sequenced. The deduced polypeptide (155 amino acid residues; molecular weight, 15,808) was highly hydrophobic and homologous to the subunits of bovine adrenal medulla, Torpedo marmorata electric lobe, Drosophila and yeast. Glu-139 (supposed to be essential for proton transport) was also conserved as the potential dicyclohexylcarbodiimide binding site. The subunit had four transmembrane segments: Segment II and IV were highly homologous and Glu-139 was located in Segment IV. The roles of the non-conserved regions are discussed.

Original languageEnglish
Pages (from-to)1062-1067
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume176
Issue number3
DOIs
Publication statusPublished - May 15 1991
Externally publishedYes

Fingerprint

Dicyclohexylcarbodiimide
Vacuolar Proton-Translocating ATPases
Torpedo
Adrenal Medulla
Cloning
Molecular Cloning
Yeast
Cerebellum
Drosophila
Protons
Complementary DNA
Yeasts
Molecular Weight
Molecular weight
Binding Sites
Amino Acids
Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H+-ATPase from mouse cerebellum. / Hanada, Hironori; Hasebe, Masahisa; Moriyama, Yoshinori; Maeda, Masatomo; Futai, Masamitsu.

In: Biochemical and Biophysical Research Communications, Vol. 176, No. 3, 15.05.1991, p. 1062-1067.

Research output: Contribution to journalArticle

Hanada, Hironori ; Hasebe, Masahisa ; Moriyama, Yoshinori ; Maeda, Masatomo ; Futai, Masamitsu. / Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H+-ATPase from mouse cerebellum. In: Biochemical and Biophysical Research Communications. 1991 ; Vol. 176, No. 3. pp. 1062-1067.
@article{0bbff5ce9e77423b86632364a1a50047,
title = "Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H+-ATPase from mouse cerebellum",
abstract = "cDNa for the 16 kDa subunit of vacuolar H+-ATPase was cloned from mouse cerebellum and sequenced. The deduced polypeptide (155 amino acid residues; molecular weight, 15,808) was highly hydrophobic and homologous to the subunits of bovine adrenal medulla, Torpedo marmorata electric lobe, Drosophila and yeast. Glu-139 (supposed to be essential for proton transport) was also conserved as the potential dicyclohexylcarbodiimide binding site. The subunit had four transmembrane segments: Segment II and IV were highly homologous and Glu-139 was located in Segment IV. The roles of the non-conserved regions are discussed.",
author = "Hironori Hanada and Masahisa Hasebe and Yoshinori Moriyama and Masatomo Maeda and Masamitsu Futai",
year = "1991",
month = "5",
day = "15",
doi = "10.1016/0006-291X(91)90391-J",
language = "English",
volume = "176",
pages = "1062--1067",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H+-ATPase from mouse cerebellum

AU - Hanada, Hironori

AU - Hasebe, Masahisa

AU - Moriyama, Yoshinori

AU - Maeda, Masatomo

AU - Futai, Masamitsu

PY - 1991/5/15

Y1 - 1991/5/15

N2 - cDNa for the 16 kDa subunit of vacuolar H+-ATPase was cloned from mouse cerebellum and sequenced. The deduced polypeptide (155 amino acid residues; molecular weight, 15,808) was highly hydrophobic and homologous to the subunits of bovine adrenal medulla, Torpedo marmorata electric lobe, Drosophila and yeast. Glu-139 (supposed to be essential for proton transport) was also conserved as the potential dicyclohexylcarbodiimide binding site. The subunit had four transmembrane segments: Segment II and IV were highly homologous and Glu-139 was located in Segment IV. The roles of the non-conserved regions are discussed.

AB - cDNa for the 16 kDa subunit of vacuolar H+-ATPase was cloned from mouse cerebellum and sequenced. The deduced polypeptide (155 amino acid residues; molecular weight, 15,808) was highly hydrophobic and homologous to the subunits of bovine adrenal medulla, Torpedo marmorata electric lobe, Drosophila and yeast. Glu-139 (supposed to be essential for proton transport) was also conserved as the potential dicyclohexylcarbodiimide binding site. The subunit had four transmembrane segments: Segment II and IV were highly homologous and Glu-139 was located in Segment IV. The roles of the non-conserved regions are discussed.

UR - http://www.scopus.com/inward/record.url?scp=0025820672&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025820672&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(91)90391-J

DO - 10.1016/0006-291X(91)90391-J

M3 - Article

VL - 176

SP - 1062

EP - 1067

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -