Involvement of a putative substrate binding site in the biogenesis and assembly of phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae

Francesca Di Bartolomeo, Kim Nguyen Doan, Karin Athenstaedt*, Thomas Becker, Günther Daum

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

In the yeast Saccharomyces cerevisiae, the mitochondrial phosphatidylserine decarboxylase 1 (Psd1p) produces the largest amount of cellular phosphatidylethanolamine (PE). Psd1p is synthesized as a larger precursor on cytosolic ribosomes and then imported into mitochondria in a three-step processing event leading to the formation of an α-subunit and a β-subunit. The α-subunit harbors a highly conserved motif, which was proposed to be involved in phosphatidylserine (PS) binding. Here, we present a molecular analysis of this consensus motif for the function of Psd1p by using Psd1p variants bearing either deletions or point mutations in this region. Our data show that mutations in this motif affect processing and stability of Psd1p, and consequently the enzyme's activity. Thus, we conclude that this consensus motif is essential for structural integrity and processing of Psd1p.

Original languageEnglish
Pages (from-to)716-725
Number of pages10
JournalBiochimica et Biophysica Acta / Molecular and Cell Biology of Lipids
Volume1862
Issue number7
DOIs
Publication statusPublished - 1 Jul 2017

Keywords

  • Mitochondria
  • Phosphatidylethanolamine
  • Phosphatidylserine decarboxylase 1
  • Phospholipid
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cooperations

  • NAWI Graz

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