Rinnerthaler, M. and Buttner, S. and Laun, P. and Heeren, G. and Felder, T. K. and Klinger, H. and Weinberger, M. and Stolze, K. and Grousl, T. and Hasek, J. and Benada, O. and Frydlova, I. and Klocker, A. and Simon-Nobbe, B. and Jansko, B. and Breitenbach-Koller, H. and Eisenberg, T. and Gourlay, C. W. and Madeo, F. and Burhans, W. C. and Breitenbach, M. (2012) Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast. Proceedings of the National Academy of Sciences, 109 (22). pp. 8658-8663. ISSN 0027-8424.
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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, AIM14) 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.
|Uncontrolled keywords:||cell cycle; integral membrane reductase; wiskostatin; latrunculin|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||08 Oct 2012 11:22|
|Last Modified:||30 Jan 2013 10:33|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/31359 (The current URI for this page, for reference purposes)|
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