The COP9 signalosome is involved in the regulation of lipid metabolism and of transition metals uptake in Saccharomyces cerevisiae. (25th November 2013)
- Record Type:
- Journal Article
- Title:
- The COP9 signalosome is involved in the regulation of lipid metabolism and of transition metals uptake in Saccharomyces cerevisiae. (25th November 2013)
- Main Title:
- The COP9 signalosome is involved in the regulation of lipid metabolism and of transition metals uptake in Saccharomyces cerevisiae
- Authors:
- Licursi, Valerio
Salvi, Chiara
De Cesare, Virginia
Rinaldi, Teresa
Mattei, Benedetta
Fabbri, Claudia
Serino, Giovanna
Bramasole, Laylan
Zimbler, Jacob Z.
Pick, Elah
Barnes, Brett M.
Bard, Martin
Negri, Rodolfo - Abstract:
- <abstract abstract-type="main" id="febs12584-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The COP9 signalosome (CSN) is a highly conserved eukaryotic protein complex which regulates the cullin RING family of ubiquitin ligases and carries out a deneddylase activity that resides in subunit 5 (CSN5). Whereas CSN activity is essential for the development of higher eukaryotes, several unicellular fungi including the budding yeast <italic>Saccharomyces cerevisiae</italic> can survive without a functional CSN. Nevertheless, the budding yeast CSN is biochemically active and deletion mutants of each of its subunits exhibit deficiency in cullins deneddylation, although the biological context of this activity is still unknown in this organism. To further characterize CSN function in budding yeast, we present here a transcriptomic and proteomic analysis of a <italic>S. cerevisiae</italic> strain deleted in the <italic>CSN5/RRI1</italic> gene (hereafter referred to as <italic>CSN5</italic>), coding for the only canonical subunit of the complex. We show that Csn5 is involved in modulation of the genes controlling amino acid and lipid metabolism and especially ergosterol biosynthesis. These alterations in gene expression correlate with the lower ergosterol levels and increased intracellular zinc content which we observed in <italic>csn5</italic> null mutant cells. We show that some of these regulatory effects of Csn5, in particular the control of isoprenoid<abstract abstract-type="main" id="febs12584-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The COP9 signalosome (CSN) is a highly conserved eukaryotic protein complex which regulates the cullin RING family of ubiquitin ligases and carries out a deneddylase activity that resides in subunit 5 (CSN5). Whereas CSN activity is essential for the development of higher eukaryotes, several unicellular fungi including the budding yeast <italic>Saccharomyces cerevisiae</italic> can survive without a functional CSN. Nevertheless, the budding yeast CSN is biochemically active and deletion mutants of each of its subunits exhibit deficiency in cullins deneddylation, although the biological context of this activity is still unknown in this organism. To further characterize CSN function in budding yeast, we present here a transcriptomic and proteomic analysis of a <italic>S. cerevisiae</italic> strain deleted in the <italic>CSN5/RRI1</italic> gene (hereafter referred to as <italic>CSN5</italic>), coding for the only canonical subunit of the complex. We show that Csn5 is involved in modulation of the genes controlling amino acid and lipid metabolism and especially ergosterol biosynthesis. These alterations in gene expression correlate with the lower ergosterol levels and increased intracellular zinc content which we observed in <italic>csn5</italic> null mutant cells. We show that some of these regulatory effects of Csn5, in particular the control of isoprenoid biosynthesis, are conserved through evolution, since similar transcriptomic and/or proteomic effects of <italic>csn5</italic> mutation were previously observed in other eukaryotic organisms such as <italic>Aspergillus nidulans</italic>, <italic> Arabidopsis thaliana</italic> and <italic>Drosophila melanogaster</italic>. Our results suggest that the diverged budding yeast CSN is more conserved than was previously thought.</p> </abstract> … (more)
- Is Part Of:
- FEBS journal. Volume 281:Number 1(2014)
- Journal:
- FEBS journal
- Issue:
- Volume 281:Number 1(2014)
- Issue Display:
- Volume 281, Issue 1 (2014)
- Year:
- 2014
- Volume:
- 281
- Issue:
- 1
- Issue Sort Value:
- 2014-0281-0001-0000
- Page Start:
- 175
- Page End:
- 190
- Publication Date:
- 2013-11-25
- Subjects:
- Biochemistry -- Periodicals
Molecular biology -- Periodicals
Pathology, Molecular -- Periodicals
572 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://gateway.ovid.com/ovidweb.cgi?T=JS&MODE=ovid&NEWS=n&PAGE=toc&D=ovft&AN=01038983-000000000-00000 ↗
http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=ejb ↗
http://onlinelibrary.wiley.com/ ↗
http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=ejb ↗ - DOI:
- 10.1111/febs.12584 ↗
- Languages:
- English
- ISSNs:
- 1742-464X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3901.578500
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