Phosphatidylethanolamine made in the inner mitochondrial membrane is essential for yeast cytochrome bc1 complex function

Elizabeth Calzada, Erica Avery, Pingdewinde N. Sam, Arnab Modak, Chunyan Wang, J. Michael McCaffery, Xianlin Han, Nathan N. Alder and Steven M. Claypool ()
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Elizabeth Calzada: Johns Hopkins University School of Medicine
Erica Avery: Johns Hopkins University School of Medicine
Pingdewinde N. Sam: Johns Hopkins University School of Medicine
Arnab Modak: University of Connecticut
Chunyan Wang: University of Texas Health Science Center at San Antonio
J. Michael McCaffery: Johns Hopkins University
Xianlin Han: University of Texas Health Science Center at San Antonio
Nathan N. Alder: University of Connecticut
Steven M. Claypool: Johns Hopkins University School of Medicine

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract Of the four separate PE biosynthetic pathways in eukaryotes, one occurs in the mitochondrial inner membrane (IM) and is executed by phosphatidylserine decarboxylase (Psd1). Deletion of Psd1 is lethal in mice and compromises mitochondrial function. We hypothesize that this reflects inefficient import of non-mitochondrial PE into the IM. Here, we test this by re-wiring PE metabolism in yeast by re-directing Psd1 to the outer mitochondrial membrane or the endomembrane system and show that PE can cross the IMS in both directions. Nonetheless, PE synthesis in the IM is critical for cytochrome bc1 complex (III) function and mutations predicted to disrupt a conserved PE-binding site in the complex III subunit, Qcr7, impair complex III activity similar to PSD1 deletion. Collectively, these data challenge the current dogma of PE trafficking and demonstrate that PE made in the IM by Psd1 support the intrinsic functionality of complex III.

Date: 2019
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DOI: 10.1038/s41467-019-09425-1

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