Identification and characterization of the mitochondrial membrane sorting signals in phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae

Ariane Wagner, Francesca Di Bartolomeo, Isabella Klein, Claudia Hrastnik, Kim Nguyen Doan, Thomas Becker, Günther Daum

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Phosphatidylserine decarboxylase 1 (Psd1p) catalyzes the formation of the majority of phosphatidylethanolamine (PE) in the yeast Saccharomyces cerevisiae. Psd1p is localized to mitochondria, anchored to the inner mitochondrial membrane (IMM) through membrane spanning domains and oriented towards the mitochondrial intermembrane space. We found that Psd1p harbors at least two inner membrane-associated domains, which we named IM1 and IM2. IM1 is important for proper orientation of Psd1p within the IMM (Horvath et al., J. Biol. Chem. 287 (2012) 36744–55), whereas it remained unclear whether IM2 is important for membrane-association of Psd1p. To discover the role of IM2 in Psd1p import, processing and assembly into the mitochondria, we constructed Psd1p variants with deletions in IM2. Removal of the complete IM2 led to an altered topology of the protein with the soluble domain exposed to the matrix and to decreased enzyme activity. Psd1p variants lacking portions of the N-terminal moiety of IM2 were inserted into IMM with an altered topology. Psd1p variants with deletions of C-terminal portions of IM2 accumulated at the outer mitochondrial membrane and lost their enzyme activity. In conclusion we showed that IM2 is essential for full enzymatic activity, maturation and correct integration of yeast Psd1p into the inner mitochondrial membrane.

Original languageEnglish
Pages (from-to)117-125
Number of pages9
JournalBiochimica et Biophysica Acta / Molecular and Cell Biology of Lipids
Volume1863
Issue number2
DOIs
Publication statusPublished - 1 Feb 2018

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Mitochondrial Membranes
Saccharomyces cerevisiae
Membranes
Mitochondria
Yeasts
Enzymes
phosphatidylserine decarboxylase
Proteins

Keywords

  • Membrane anchor
  • Phosphatidylethanolamine
  • Phosphatidylserine
  • Phosphatidylserine decarboxylase
  • S. cerevisiae

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Identification and characterization of the mitochondrial membrane sorting signals in phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae. / Wagner, Ariane; Di Bartolomeo, Francesca; Klein, Isabella; Hrastnik, Claudia; Doan, Kim Nguyen; Becker, Thomas; Daum, Günther.

In: Biochimica et Biophysica Acta / Molecular and Cell Biology of Lipids, Vol. 1863, No. 2, 01.02.2018, p. 117-125.

Research output: Contribution to journalArticleResearchpeer-review

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abstract = "Phosphatidylserine decarboxylase 1 (Psd1p) catalyzes the formation of the majority of phosphatidylethanolamine (PE) in the yeast Saccharomyces cerevisiae. Psd1p is localized to mitochondria, anchored to the inner mitochondrial membrane (IMM) through membrane spanning domains and oriented towards the mitochondrial intermembrane space. We found that Psd1p harbors at least two inner membrane-associated domains, which we named IM1 and IM2. IM1 is important for proper orientation of Psd1p within the IMM (Horvath et al., J. Biol. Chem. 287 (2012) 36744–55), whereas it remained unclear whether IM2 is important for membrane-association of Psd1p. To discover the role of IM2 in Psd1p import, processing and assembly into the mitochondria, we constructed Psd1p variants with deletions in IM2. Removal of the complete IM2 led to an altered topology of the protein with the soluble domain exposed to the matrix and to decreased enzyme activity. Psd1p variants lacking portions of the N-terminal moiety of IM2 were inserted into IMM with an altered topology. Psd1p variants with deletions of C-terminal portions of IM2 accumulated at the outer mitochondrial membrane and lost their enzyme activity. In conclusion we showed that IM2 is essential for full enzymatic activity, maturation and correct integration of yeast Psd1p into the inner mitochondrial membrane.",
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