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Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast
Mark Rinnerthaler, Sabrina Büttner, Peter Laun, Gino Heeren, Thomas K. Felder, Harald Klinger, Martin Weinberger, Klaus Stolze, Tomas Grousl, Jiri Hasek, Oldrich Benada, Ivana Frydlova, Andrea Klocker, Birgit Simon-Nobbe, Bettina Jansko, Hannelore Breitenbach-Koller, Tobias Eisenberg, Campbell W. Gourlay, Frank Madeo, William C. Burhans and Michael Breitenbach
Proceedings of the National Academy of Sciences of the United States of America
Vol. 109, No. 22 (May 29, 2012), pp. 8658-8663
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/41602611
Page Count: 6
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The large protein superfamily of NADPH oxidases (NOX enzymes) is found in members of all eukaryotic kingdoms: animals, plants, fungi, and protists. The physiological functions of these NOX enzymes range from defense to specialized oxidative biosynthesis and to signaling. In filamentous fungi, NOX enzymes are involved in signaling cell differentiation, in particular in the formation of fruiting bodies. On the basis of bioinformatics analysis, until now it was believed that the genomes of unicellular fungi like Saccharomyces cerevisiae and Schizosaccharomyces pombe do not harbor genes coding for NOX enzymes. Nevertheless, the genome of S. cerevisiae contains nine ORFs showing sequence similarity to the catalytic subunits of mammalian NOX enzymes, only some of which have been functionally assigned as ferric reductases involved in iron ion transport. Here we show that one of the nine ORFs (YGL160W, AIM 14) encodes a genuine NADPH oxidase, which is located in the endoplasmic reticulum (ER) and produces superoxide in a NADPH-dependent fashion. We renamed this ORF YNO1 (yeast NADPH oxidase 1). Overexpression of YNO1 causes YCA1-dependent apoptosis, whereas deletion of the gene makes cells less sensitive to apoptotic stimuli. Several independent lines of evidence point to regulation of the actin cytoskeleton by reactive oxygen species (ROS) produced by Yno1p.
Proceedings of the National Academy of Sciences of the United States of America © 2012 National Academy of Sciences