Expression of mammalian mitochondrial F1-ATPase in Escherichia coli depends on two chaperone factors, AF1 and AF2

Toshiharu Suzuki, Naoya Iida, Junko Suzuki, Yasunori Watanabe, Toshiya Endo, Toru Hisabori, Masasuke Yoshida

Research output: Contribution to journalArticle

Abstract

F1-ATPase (F1) is a multisubunit water-soluble domain of FoF1-ATP synthase and is a rotary enzyme by itself. Earlier genetic studies using yeast suggested that two factors, Atp11p and Atp12p, contribute to F1 assembly. Here, we show that their mammalian counterparts, AF1 and AF2, are essential and sufficient for efficient production of recombinant bovine mitochondrial F1 in Escherichia coli cells. Intactness of the function and conformation of the E. coli-expressed bovine F1 was verified by rotation analysis and crystallization. This expression system opens a way for the previously unattempted mutation study of mammalian mitochondrial F1.

Original languageEnglish
Pages (from-to)1267-1272
Number of pages6
JournalFEBS Open Bio
Volume6
Issue number12
DOIs
Publication statusPublished - 2016 Dec 1

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Proton-Translocating ATPases
Escherichia coli
Open systems
Crystallization
Yeast
Conformations
Adenosine Triphosphate
Yeasts
Mutation
Water
Enzymes
factor AF2

Keywords

  • F-ATPase
  • FF-ATP synthase
  • molecular chaperone

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Expression of mammalian mitochondrial F1-ATPase in Escherichia coli depends on two chaperone factors, AF1 and AF2. / Suzuki, Toshiharu; Iida, Naoya; Suzuki, Junko; Watanabe, Yasunori; Endo, Toshiya; Hisabori, Toru; Yoshida, Masasuke.

In: FEBS Open Bio, Vol. 6, No. 12, 01.12.2016, p. 1267-1272.

Research output: Contribution to journalArticle

Suzuki, Toshiharu ; Iida, Naoya ; Suzuki, Junko ; Watanabe, Yasunori ; Endo, Toshiya ; Hisabori, Toru ; Yoshida, Masasuke. / Expression of mammalian mitochondrial F1-ATPase in Escherichia coli depends on two chaperone factors, AF1 and AF2. In: FEBS Open Bio. 2016 ; Vol. 6, No. 12. pp. 1267-1272.
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