Metalloregulation of FRE1 and FRE2Homologs in Saccharomyces cerevisiae

Martins, Laura J.; Jensen, Laran T.; Simon, Jay R.; Keller, Greg; Winge, Dennis R.

doi:10.1074/jbc.273.37.23716

Cited by 181 publications

(153 citation statements)

References 31 publications

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“…1). Three of the four motifs were immediately preceded by 59 TTT 39 , making them identical to cis-acting copper response elements (CuREs) found in the promoters of CTR1, CTR3, FRE1 and FRE7 of S. cerevisiae (Labbe et al, 1997;Yamaguchi-Iwai et al, 1997;Martins et al, 1998). The core sequence of these transcription Transposon insertions mapped within a 1?1 kb EcoRI fragment are denoted as double-headed horizontal black arrows at nucleotides 122, 134 and 658.…”

Section: Resultsmentioning

confidence: 99%

“…Analysis of the CaCTR1 promoter sequence revealed four sequences resembling the S. cerevisiae copper response elements (CuREs). These motifs facilitate binding of the copper-sensing transactivator Mac1p (Dancis et al, 1992;Jungmann et al, 1993;Yamaguchi-Iwai et al, 1997;Labbe et al, 1997;Martins et al, 1998). The presence of CuRE-like elements in the promoter of CaCTR1 may explain how expression of the gene is controlled in response to copper availability in S. cerevisiae by the copper-sensing transactivator Mac1p.…”

Section: Discussionmentioning

confidence: 99%

“…more efficient binding of a putative transactivator to these sequences. In S. cerevisiae the distance between the motifs has also been shown to have a limited effect on transcription, with greater spacing attenuating expression (Martins et al, 1998). Therefore the two C. albicans putative CuRE motifs with the least distance between them (2268 to 278 and 2239 to 2229) are the stronger candidates to facilitate the most effective transcriptional control.…”

Section: Discussionmentioning

confidence: 99%

“…The copper-responsive activator Mac1p regulates FRE1, CTR1, CTR3 and FRE7, the uncharacterized homologue of FRE1, while the iron-responsive activator Aft1p regulates FRE1, FRE2, FRE3-6, FTR1, FET3, ATX1, CCC2, and a family of intracellular siderophore transporter genes ARN1-4 (Dancis et al, 1992;Lin et al, 1997;Jungmann et al, 1993;Yamaguchi-Iwai et al, 1996;Labbe et al, 1997;Martins et al, 1998;Lesuisse et al, 1998;Heymann et al, 2000;Yun et al, 2000a, b). Thus FRE1 is regulated by both copper and iron through the activity of Mac1p and Aft1p, whereas the copper-trafficking genes ATX1 and CCC2 are regulated by iron through the activity of Aft1p.…”

Section: Introductionmentioning

confidence: 99%

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The Candida albicans CTR1 gene encodes a functional copper transporter

2003

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Copper and iron uptake in Saccharomyces cerevisiae are linked through a high-affinity ferric/cupric-reductive uptake system. Evidence suggests that a similar system operates in Candida albicans. The authors have identified a C. albicans gene that is able to rescue a S. cerevisiae ctr1/ctr3-null mutant defective in high-affinity copper uptake. The 756 bp ORF, designated CaCTR1, encodes a 251 amino acid protein with a molecular mass of 27·8 kDa. Comparisons between the deduced amino acid sequence of the C. albicans Ctr1p and S. cerevisiae Ctr1p indicated that they share 39·6 % similarity and 33·0 % identity over their entire length. Within the predicted protein product of CaCTR1 there are putative transmembrane regions and sequences that resemble copper-binding motifs. The promoter region of CaCTR1 contains four sequences with significant identity to S. cerevisiae copper response elements. CaCTR1 is transcriptionally regulated in S. cerevisiae in response to copper availability by the copper-sensing transactivator Mac1p. Transcription of CaCTR1 in C. albicans is also regulated in a copper-responsive manner. This raises the possibility that CaCTR1 may be regulated in C. albicans by a Mac1p-like transactivator. A C. albicans ctr1-null mutant displays phenotypes consistent with the lack of copper uptake including growth defects in low-copper and low-iron conditions, a respiratory deficiency and sensitivity to oxidative stress. Furthermore, changes in morphology were observed in the C. albicans ctr1-null mutant. It is proposed that CaCTR1 facilitates transport of copper into the cell.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The Candida albicans CTR1 gene encodes a functional copper transporter

2003

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“…S1). A ferric reductase function has been shown for FRE1-FRE4 (17), and iron-(or copper)-dependent transcriptional control was found for FRE1-FRE7 (18,19). FRE8 and YNO1 cluster together and are neither transcriptionally controlled by iron nor is the deletion dependent on increased iron for growth (18).…”

Section: Resultsmentioning

confidence: 99%

Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast

Rinnerthaler

Büttner

Laun

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

131

136

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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.cell cycle | integral membrane reductase | wiskostatin | latrunculin R eactive oxygen species (ROS) have multiple roles in physiology and pathophysiology, in particular during aging and induction of programmed cell death. This includes also nonmitochondrial sources, besides the long-studied mitochondrially generated ROS. These findings can be viewed as important additions to the classical "free radical theory of aging" (1) and theories developed thereafter (2, 3).In higher organisms, among others, at least two major sources of superoxide other than mitochondria are known. On the one hand, xanthine oxidase, an enzyme in the catabolism of purines, which catalyses the oxidation of hypoxanthine to xanthine and to uric acid, produces superoxide (4). On the other hand, NADPH oxidases (NOX) catalyze the production of superoxide from oxygen and NADPH (5).The NADPH oxidase superfamily of membrane-located enzymes of higher cells has been known for a decade (for review, ref. 5). Whereas the human NOX2 was discovered early on, other NOX (Nox1/3/4/5) as well as dual oxidase (DUOX) (Duox1/2) enzymes (displaying two domains: a NADPH oxidase domain and a peroxidase domain) have been found relatively recently in human cells. The human NOX2 was discovered as a defense enzyme of neutrophils and macrophages, which produce a burst of superoxide (O 2 · − ) as a first line of defense against invading microorganisms. Although X-ray or NMR structure determinations are not available, we know from indirect evidence and bioinformatics that the catalytic subunit of the macrophage enzyme contains six transmembrane helices, is located in the plasma membrane, and produces superoxide in a vectorial ...

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Iron Uptake by Plants and Fungi

Crichton

2009

Iron Metabolism

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Metalloregulation of FRE1 and FRE2Homologs in Saccharomyces cerevisiae

Abstract: The high affinity uptake systems for iron and copper ions in Saccharomyces cerevisiae involve metal-specific permeases and two known cell surface Cu(II) and Fe (

Cited by 181 publications

References 31 publications

The Candida albicans CTR1 gene encodes a functional copper transporter

The Candida albicans CTR1 gene encodes a functional copper transporter

Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast

Iron Uptake by Plants and Fungi

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