tailieunhanh - Báo cáo khoa học: Lpe10p modulates the activity of the Mrs2p-based yeast mitochondrial Mg2+channel

Saccharomyces cerevisiaeLpe10p is a homologue of the Mg 2+ -channel-forming protein Mrs2p in the inner mitochondrial membrane. Deletion of MRS2, LPE10or both results in a petite phenotype, which exhibits a respi-ratory growth defect on nonfermentable carbon sources. Only coexpression ofMRS2andLPE10leads to full complementation of the mrs2D⁄lpe10D double disruption, indicating that these two proteins cannot substitute for each other. | Lpe10p modulates the activity of the Mrs2p-based yeast mitochondrial Mg2 channel Gerhard Sponder1 Sona Svidova1 Rainer Schindl2 Stefan Wieser2 Rudolf J. Schweyen1 Christoph Romanin2 Elisabeth M. Froschauer1 and Julian Weghuber2 1 Max F. Perutz Laboratories Department of Microbiology Immunology and Genetics Vienna Austria 2 Institute of Biophysics University of Linz Austria Keywords membrane potential Mg2 -channel mitochondria oligomerization single-channel patch clamp Correspondence J. Weghuber Institute of Biophysics University of Linz AltenbergerstraBe 69 4040 Linz Austria Fax 43 732 2468 29284 Tel 43 732 2468 9266 E-mail These authors contributed equally to this work Note This paper is dedicated to the memory of Rudolf Schweyen who tragically died during the preparation of the manuscript Received 20 April 2010 revised 28 May 2010 accepted 1 July 2010 doi Saccharomyces cerevisiae Lpe10p is a homologue of the Mg2 -channelforming 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 mrs2D lpe10D 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 Mg2 influx into mitochondria as has been reported for MRS2 deletion. Additionally we found a considerable loss of the mitochondrial membrane potential AW in the absence of Lpe10p which was not detected in mrs2D cells. Addition of the K H -exchanger nigericin which artificially increases AW led to restoration of Mg2 influx into mitochondria in lpe10A cells but not in mrs2A lpe10A cells. Mutational analysis of Lpe10p and domain swaps between Mrs2p and Lpe10p suggested that the maintenance of AW and that of Mg2 influx are functionally separated. Crosslinking and Blue .

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