Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life

Yang Xu, Ashim Malhotra, Steven M Claypool, Mindong Ren, Michael Schlame

Research output: Contribution to journalArticle

Abstract

Tafazzin is a transacylase that affects cardiolipin fatty acid composition and mitochondrial function. Mutations in human tafazzin cause Barth syndrome yet the enzyme has mostly been characterized in yeast. To study tafazzin in higher organisms, we isolated mitochondria from Drosophila and mammalian cell cultures. Our data indicate that tafazzin binds to multiple protein complexes in these organisms, and that the interactions of tafazzin lack strong specificity. Very large tafazzin complexes could only be detected in the presence of cardiolipin, but smaller complexes remained intact even upon treatment with phospholipase A2. In mammalian cells, tafazzin had a half-life of only 3-6h, which was much shorter than the half-life of other mitochondrial proteins. The data suggest that tafazzin is a transient resident of multiple protein complexes.

Original languageEnglish (US)
Pages (from-to)27-32
Number of pages6
JournalMitochondrion
Volume21
DOIs
StatePublished - Mar 1 2015

Fingerprint

Cardiolipins
Drosophila
Half-Life
Barth Syndrome
Phospholipases A2
Mitochondrial Proteins
Mitochondria
Proteins
Fatty Acids
Cell Culture Techniques
Yeasts
Mutation
Enzymes

Keywords

  • Barth syndrome
  • Cardiolipin
  • Membrane assembly
  • Mitochondria
  • Protein complex
  • Tafazzin

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Molecular Medicine

Cite this

Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life. / Xu, Yang; Malhotra, Ashim; Claypool, Steven M; Ren, Mindong; Schlame, Michael.

In: Mitochondrion, Vol. 21, 01.03.2015, p. 27-32.

Research output: Contribution to journalArticle

Xu, Yang ; Malhotra, Ashim ; Claypool, Steven M ; Ren, Mindong ; Schlame, Michael. / Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life. In: Mitochondrion. 2015 ; Vol. 21. pp. 27-32.
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