Metal Acquisition and Availability in the Mitochondria

Atkinson, Aaron; Winge, Dennis R.

doi:10.1021/cr900006y

Cited by 128 publications

(74 citation statements)

References 174 publications

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“…The donor for iron has not been definitely established. Likewise, the physiological forms of imported and/or stored iron are unknown (46). However, reduced iron (ferrous) seems to 4 A. Dancis and D. Pain, unpublished observations.…”

Section: Discussionmentioning

confidence: 99%

Mitochondrial NADH Kinase, Pos5p, Is Required for Efficient Iron-Sulfur Cluster Biogenesis in Saccharomyces cerevisiae

Pain

Balamurali

Dancis

et al. 2010

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Mitochondrial NADH Kinase, Pos5p, Is Required for Efficient Iron-Sulfur Cluster Biogenesis in Saccharomyces cerevisiae

Pain

Balamurali

Dancis

et al. 2010

Journal of Biological Chemistry

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“…Impaired bc 1 Complex Activity Was Corroborated by Analysis of the Respiratory Complexes-Dodecyl maltoside solubilization reduces supercomplexes to individual complexes that can be separated by BN-PAGE. Visualization of the bc 1 complex using antibodies to three separate subunits revealed its attenuation in mzm1⌬ cells (Fig.…”

Section: High-throughput Screen Of Yeast Deletion Strains For Attenuamentioning

confidence: 99%

“…The zinc mitochondrial metalloproteome is large relative to other metals and distributed throughout the organelle (1). The zinc proteome is heavily populated by proteases and in yeast include the iAAA, mAAA, Oma1, Oct1, Icp55, Atp23, and the MPP protease complex.…”

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confidence: 99%

Mzm1 Influences a Labile Pool of Mitochondrial Zinc Important for Respiratory Function

Atkinson

Khalimonchuk

Smith

et al. 2010

Journal of Biological Chemistry

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Zinc is essential for function of mitochondria as a cofactor for several matrix zinc metalloproteins. We demonstrate that a labile cationic zinc component of low molecular mass exists in the yeast mitochondrial matrix. This zinc pool is homeostatically regulated in response to the cellular zinc status. This pool of zinc is functionally important because matrix targeting of a cytosolic zinc-binding protein reduces the level of labile zinc and interferes with mitochondrial respiratory function. We identified a series of proteins that modulate the matrix zinc pool, one of which is a novel conserved mitochondrial protein designated Mzm1. Mutant mzm1⌬ cells have reduced total and labile mitochondrial zinc, and these cells are hypersensitive to perturbations of the labile pool. In addition, mzm1⌬ cells have a destabilized cytochrome c reductase (Complex III) without any effects on Complexes IV or V. Thus, we have established that a link exists between Complex III integrity and the labile mitochondrial zinc pool.All known mitochondrial zinc-requiring metalloproteins are synthesized in the cytoplasm and must be imported as newly synthesized polypeptides into the organelle as with most resident proteins. Protein import into the mitochondria requires unfolded polypeptides, so folding and metallation occur upon import. Thus, a bioavailable pool of Zn(II) must be maintained within the mitochondria for efficient metallation reactions. The folding of metalloproteins is dependent on the availability and the selective insertion of the appropriate metal ion. Mis-metallation by a non-native metal ion may be deleterious yielding either an inactive protein or a misfolded state prone to aggregation.The zinc mitochondrial metalloproteome is large relative to other metals and distributed throughout the organelle (1). The zinc proteome is heavily populated by proteases and in yeast include the iAAA, mAAA, Oma1, Oct1, Icp55, Atp23, and the MPP protease complex. These proteases all share an essential HEXXH or HXXEH metal-binding motif and whereas many metalloproteinases can be activated in vitro by diverse divalent cations, Zn(II) is likely to be the physiological metal ion bound.Zn(II) is an abundant cofactor for a variety of additional metalloenzymes in mitochondria, including Adh3, Adh4, and

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“…Iron(III) is an important metal ion in living organisms; Fe 3+ and its complexes are present in hemoglobin, myoglobin, heme enzymes and in other cofactors essential in the reactivity of biological species; it is involved in cellular energy regeneration processes [1][2][3][4]. The accumulation of large amounts of iron(III) in the body causes several heart malfunctions and may be the origin of other diseases such as cancer and haemochromatosis.…”

Section: Introductionmentioning

confidence: 99%

Comparison of polysiloxane films substituted by undecenyl-cyclam and by naphthyl-cyclam for the design of ISFET devices sensitive to Fe3+ ions

Mefteh

Touzi

Chevalier

et al. 2014

Sensors and Actuators B: Chemical

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Metal Acquisition and Availability in the Mitochondria

Cited by 128 publications

References 174 publications

Mitochondrial NADH Kinase, Pos5p, Is Required for Efficient Iron-Sulfur Cluster Biogenesis in Saccharomyces cerevisiae

Mitochondrial NADH Kinase, Pos5p, Is Required for Efficient Iron-Sulfur Cluster Biogenesis in Saccharomyces cerevisiae

Mzm1 Influences a Labile Pool of Mitochondrial Zinc Important for Respiratory Function

Comparison of polysiloxane films substituted by undecenyl-cyclam and by naphthyl-cyclam for the design of ISFET devices sensitive to Fe3+ ions

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