Lpe10p modulates the activity of the Mrs2p-based yeast mitochondrial Mg2+ channel

The FEBS Journal
Gerhard SponderJulian Weghuber

Abstract

Saccharomyces cerevisiae Lpe10p is a homologue of the Mg(2+)-channel-forming protein Mrs2p in the inner mitochondrial membrane. Deletion of MRS2, LPE10 or both results in a petite phenotype, which exhibits a respiratory growth defect on nonfermentable carbon sources. Only coexpression of MRS2 and LPE10 leads to full complementation of the mrs2Delta/lpe10Delta double disruption, indicating that these two proteins cannot substitute for each other. Here, we show that deletion of LPE10 results in a loss of rapid Mg(2+) influx into mitochondria, as has been reported for MRS2 deletion. Additionally, we found a considerable loss of the mitochondrial membrane potential (DeltaPsi) in the absence of Lpe10p, which was not detected in mrs2Delta cells. Addition of the K(+)/H(+)-exchanger nigericin, which artificially increases DeltaPsi, led to restoration of Mg(2+) influx into mitochondria in lpe10Delta cells, but not in mrs2Delta/lpe10Delta cells. Mutational analysis of Lpe10p and domain swaps between Mrs2p and Lpe10p suggested that the maintenance of DeltaPsi and that of Mg(2+) influx are functionally separated. Cross-linking and Blue native PAGE experiments indicated interaction of Lpe10p with the Mrs2p-containing channel complex. Using ...Continue Reading

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Citations

Aug 21, 2013·Biochimica Et Biophysica Acta·Jian PayandehEmil F Pai
Jan 15, 2015·Biochimica Et Biophysica Acta·Yixian CuiBing Zhou
Apr 3, 2014·Physiological Reviews·Ildiko Szabo, Mario Zoratti
Jul 9, 2020·Synthetic and Systems Biotechnology·Xuan CaoYongjin J Zhou

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