کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2068674 1544423 2015 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیوفیزیک
پیش نمایش صفحه اول مقاله
Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life
چکیده انگلیسی


• Tafazzin binds to multiple protein complexes in mitochondria and microsomes of Drosophila.
• Tafazzin binds to multiple protein complexes in mitochondria of mammalian cells.
• Tafazzin has a short half-life.

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 3–6 h, 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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Mitochondrion - Volume 21, March 2015, Pages 27–32
نویسندگان
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