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The phosphatidylethanolamine level of yeast mitochondria is affected by the mitochondrial components Oxa1p and Yme1p
Author(s) -
Nebauer Ruth,
Schuiki Irmgard,
Kulterer Birgit,
Trajanoski Zlatko,
Daum Günther
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06138.x
Subject(s) - phosphatidylethanolamine , translocase of the inner membrane , mitochondrial carrier , inner mitochondrial membrane , mitochondrion , atp–adp translocase , biology , microbiology and biotechnology , translocase of the outer membrane , phosphatidylserine , inner membrane , biochemistry , mitochondrial fission , mitochondrial membrane transport protein , bacterial outer membrane , phosphatidylcholine , phospholipid , membrane , gene , escherichia coli
The majority of phosphatidylethanolamine, an essential component of yeast mitochondria, is synthesized by phosphatidylserine decarboxylase 1 (Psd1p), a component of the inner mitochondrial membrane. Here, we report that deletion of OXA1 encoding an inner mitochondrial membrane protein translocase markedly affects the mitochondrial phosphatidylethanolamine level. In an oxa1Δ mutant, cellular and mitochondrial levels of phosphatidylethanolamine were lowered similar to a mutant with PSD1 deleted, and the rate of phosphatidylethanolamine synthesis by decarboxylation of phosphatidylserine in vivo and in vitro was decreased. This was due to a lower PSD1 transcription rate in the oxa1Δ mutant compared with wild‐type and compromised assembly of Psd1p into the inner mitochondrial membrane. Lack of Mba1p, another component involved in the assembly of mitochondrial proteins into the inner mitochondrial membrane, did not affect the amount of phosphatidylethanolamine or the assembly of Psd1p. Deletion of the inner membrane protease Yme1p enhanced Psd1p stability suggesting that Yme1p contributed substantially to the proteolytic turnover of Psd1p in wild‐type. In summary, our results demonstrate a link between the mitochondrial protein import machinery, assembly and stability of Psd1p, and phosphatidylethanolamine homeostasis in yeast mitochondria.